{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":5,"total":323,"mapped":5},"pagination":{"has_next":true,"next_token":"-1[]P37840,1,P37840,41,2][P10636,1,P10636,164,8]["},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"P37840","source":"P37840|Alpha-synuclein","targets":["1XQ8|Human micelle-bound alpha-synuclein|SOLUTION NMR||Homo sapiens|0|LIPID BINDING PROTEIN","2JN5|Solution Structure of a Dodecapeptide from Alpha-Synuclein Bound with Synphilin-1|SOLUTION NMR|||0|LIPID BINDING PROTEIN, PROTEIN FIBRIL","2KKW|SLAS-micelle bound alpha-synuclein|SOLUTION NMR, EPR||Homo sapiens|0|LIPID BINDING PROTEIN","2M55|NMR structure of the complex of an N-terminally acetylated alpha-synuclein peptide with calmodulin|SOLUTION NMR||Homo sapiens; SYNTHETIC CONSTRUCT|0|CALCIUM BINDING PROTEIN/PROTEIN FIBRIL","2N0A|Atomic-resolution structure of alpha-synuclein fibrils|SOLID-STATE NMR||Homo sapiens|0|STRUCTURAL PROTEIN","2X6M|Structure of a single domain camelid antibody fragment in complex with a C-terminal peptide of alpha-synuclein|X-RAY DIFFRACTION|1.62|CAMELUS DROMEDARIUS; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","3Q25|Crystal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)|X-RAY DIFFRACTION|1.9|Escherichia coli; Homo sapiens|0|SUGAR BINDING PROTEIN, PROTEIN FIBRIL","3Q26|Cyrstal structure of human alpha-synuclein (10-42) fused to maltose binding protein (MBP)|X-RAY DIFFRACTION|1.54|Escherichia coli; Homo sapiens|0|SUGAR BINDING PROTEIN, PROTEIN FIBRIL","3Q27|Cyrstal structure of human alpha-synuclein (32-57) fused to maltose binding protein (MBP)|X-RAY DIFFRACTION|1.302|Escherichia coli; Homo sapiens|0|SUGAR BINDING PROTEIN, PROTEIN FIBRIL","3Q28|Cyrstal structure of human alpha-synuclein (58-79) fused to maltose binding protein (MBP)|X-RAY DIFFRACTION|1.6|Escherichia coli; Homo sapiens|0|SUGAR BINDING PROTEIN, PROTEIN FIBRIL","3Q29|Cyrstal structure of human alpha-synuclein (1-19) fused to maltose binding protein (MBP)|X-RAY DIFFRACTION|2.3|Escherichia coli; Homo sapiens|0|SUGAR BINDING PROTEIN, PROTEIN FIBRIL","4BXL|Structure of alpha-synuclein in complex with an engineered binding protein|SOLUTION NMR||HOMO SAPIENS; SYNTHETIC CONSTRUCT|0|FIBRIL","4R0U|Tgvtava, an amyloid forming segment from alpha synuclein, residues 72-78|X-RAY DIFFRACTION|1.38||0|PROTEIN FIBRIL","4R0W|Vvtgvta, an amyloid forming segment from alpha synuclein, residues 70-76|X-RAY DIFFRACTION|1.5||0|PROTEIN FIBRIL","4RIK|Amyloid forming segment, AVVTGVTAV, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 69-77|X-RAY DIFFRACTION|1.854||0|LIPID BINDING PROTEIN","4RIL|Structure of the amyloid forming segment, GAVVTGVTAVA, from the NAC domain of Parkinson's disease protein alpha-synuclein, residues 68-78, determined by electron diffraction|ELECTRON CRYSTALLOGRAPHY|1.43||0|LIPID BINDING PROTEIN","4ZNN|MicroED structure of the segment, GVVHGVTTVA, from the A53T familial mutant of Parkinson's disease protein, alpha-synuclein residues 47-56|ELECTRON CRYSTALLOGRAPHY|1.41||0|LIPID BINDING PROTEIN","5CRW|Crystal structure of the b'-a' domain of oxidized protein disulfide isomerase complexed with alpha-synuclein peptide (31-41)|X-RAY DIFFRACTION|1.6|Humicola insolens; SYNTHETIC CONSTRUCT|0|ISOMERASE/METAL BINDING PROTEIN","6A6B|cryo-em structure of alpha-synuclein fiber|ELECTRON MICROSCOPY|3.07|Homo sapiens|0|PROTEIN FIBRIL","6CT7|Fab of anti-a-synuclein antibody BIIB054 in complex with acetylated a-synuclein peptide (1-10)|X-RAY DIFFRACTION|1.903|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6CU7|Alpha Synuclein fibril formed by full length protein - Rod Polymorph|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","6CU8|Alpha Synuclein fibril formed by full length protein - Twister Polymorph|ELECTRON MICROSCOPY|3.6|Homo sapiens|0|PROTEIN FIBRIL","6H6B|Structure of alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","6I42|Structure of the alpha-Synuclein PreNAC/Cyclophilin A-complex|X-RAY DIFFRACTION|1.38|Homo sapiens|0|ISOMERASE","6L1T|Cryo-EM structure of phosphorylated Tyr39 a-synuclein amyloid fibril|ELECTRON MICROSCOPY|3.22||0|PROTEIN FIBRIL","6L1U|Cryo-EM structure of phosphorylated Tyr39 alpha-synuclein amyloid fibril|ELECTRON MICROSCOPY|3.37||0|PROTEIN FIBRIL","6L4S|cryo-em structure of alpha-synuclein fiber mutation type E46K|ELECTRON MICROSCOPY|3.37|Homo sapiens|0|PROTEIN FIBRIL","6LRQ|Cryo-EM structure of A53T alpha-synuclein amyloid fibril|ELECTRON MICROSCOPY|3.49|Homo sapiens|0|PROTEIN FIBRIL","6OSJ|Cryo-EM structure of the N-terminally acetylated full length alpha-synuclein fibrils (Ac1-140)|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","6OSL|Cryo-EM structure of the N-terminally acetylated C-terminal Alpha-synuclein truncation Ac1-122|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","6OSM|Cryo-EM structure of the N-terminally acetylated C-terminal Alpha-synuclein truncation Ac1-103|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","6PEO|Cryo-EM structure of alpha-synuclein H50Q Narrow Fibril|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6PES|Cryo-EM structure of alpha-synuclein H50Q Wide Fibril|ELECTRON MICROSCOPY|3.6|Homo sapiens|0|PROTEIN FIBRIL","6RT0|cryo-em structure of alpha-synuclein fibril polymorph 2A|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","6RTB|cryo-em structure of alpha-synuclein fibril polymorph 2B|ELECTRON MICROSCOPY|3.46|Homo sapiens|0|PROTEIN FIBRIL","6SST|cryo-em structure of alpha-synuclein fibril polymorph 2B|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","6SSX|cryo-em structure of alpha-synuclein fibril polymorph 2A|ELECTRON MICROSCOPY|2.98|Homo sapiens|0|PROTEIN FIBRIL","6UFR|Structure of recombinantly assembled E46K alpha-synuclein fibrils|ELECTRON MICROSCOPY|2.5|Homo sapiens|0|PROTEIN FIBRIL","6XYO|Multiple system atrophy Type I alpha-synuclein filament|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|PROTEIN FIBRIL","6XYP|Multiple system atrophy Type II-1 alpha-synuclein filament|ELECTRON MICROSCOPY|3.29|Homo sapiens|0|PROTEIN FIBRIL","6XYQ|Multiple system atrophy Type II-2 alpha-synuclein filament|ELECTRON MICROSCOPY|3.09|Homo sapiens|0|PROTEIN FIBRIL","7C1D|Cryo-EM structure of the hE46K cross-seeded hWT alpha-synuclein fibril|ELECTRON MICROSCOPY|3.8|Homo sapiens|0|PROTEIN FIBRIL","7E0F|CryoEM structure of G51D alpha-synuclein amyloid fibril|ELECTRON MICROSCOPY|3.02|Homo sapiens|0|PROTEIN FIBRIL","7L7H|Alpha-synuclein fibrils|ELECTRON MICROSCOPY|4.0|Homo sapiens|0|PROTEIN FIBRIL","7LC9|Cryo-EM structure of the N-terminal alpha-synuclein truncation 41-140|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","7NCA|Type 1A alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 2|ELECTRON MICROSCOPY|3.47|Homo sapiens|0|PROTEIN FIBRIL","7NCG|Type 2A alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 2|ELECTRON MICROSCOPY|3.43|Homo sapiens|0|PROTEIN FIBRIL","7NCH|Type 1B alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 1|ELECTRON MICROSCOPY|3.84|Homo sapiens|0|PROTEIN FIBRIL","7NCI|Type 2B alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 1|ELECTRON MICROSCOPY|3.55|Homo sapiens|0|PROTEIN FIBRIL","7NCJ|Type 2AB alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 1|ELECTRON MICROSCOPY|4.23|Homo sapiens|0|PROTEIN FIBRIL","7NCK|Type 3 alpha-synuclein filament seeded in vitro by filaments purified from Multiple Systems Atrophy Case 5|ELECTRON MICROSCOPY|3.18|Homo sapiens|0|PROTEIN FIBRIL","7OZG|PMCA-amplified alpha-synuclein fibril polymorph, Parkinson's Disease patient-derived seeds|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7OZH|PMCA-amplified alpha-synuclein fibril polymorph, Multiple System Atrophy patient-derived seeds|ELECTRON MICROSCOPY|3.02|Homo sapiens|0|PROTEIN FIBRIL","7STX|Cryo-EM structure of human NatB in complex with CoA-Alpha-Synuclein|ELECTRON MICROSCOPY|3.14|Homo sapiens|0|TRANSFERASE","7UAK|Structure of recombinantly assembled A53E alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.38|Homo sapiens|0|PROTEIN FIBRIL","7V47|Type 1A alpha-synuclein fibril seeded by cerebrospinal fluid from a preclinical Parkinson's disease patient|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7V48|Type 1D alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7V49|Type 4 alpha-synuclein fibril seeded by cerebrospinal fluid from a postmortal Parkinson's disease patient|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7V4A|Heparin-induced alpha-synuclein fibrils polymorph 1|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","7V4B|Heparin-induced alpha-synuclein fibrils polymorph 3|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","7V4C|Heparin-induced alpha-synuclein fibrils polymorph 4|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7V4D|Heparin-remodelled alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","7WMM|alpha-synuclein fibril-F0502B complex|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|PROTEIN FIBRIL","7WNZ|CryoEM structure of human alpha-synuclein A53T fibril|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7WO0|CryoEM structure of human alpha-synuclein A53T fibril induced by calcium ions|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN FIBRIL","7XJX|The cryo-EM structure of Fe3+ induced alpha-syn fibril.|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN FIBRIL","7XO0|Minor polymorph inalpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-1) Parkinson's disease patient|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7XO1|Major polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-1) Parkinson's disease patient|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7XO2|Minor polymorph in alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-4) Parkinson's disease patient|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7XO3|Type 1C alpha-synuclein fibril seeded by cerebrospinal fluid from a mid-to-late stage (mid-PD-4) Parkinson's disease patient|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|PROTEIN FIBRIL","7YK2|Cryo-EM structure of Apo-alpha-syn fibril|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7YK8|Cryo-EM structure of dLAG3-alpha-syn fibril|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7YNF|CCA-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|2.5|Homo sapiens|0|PROTEIN FIBRIL","7YNG|CR-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","7YNL|EB-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|PROTEIN FIBRIL","7YNM|ThT-bound alpha-synuclein fibrils conformation 1|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN FIBRIL","7YNN|ThT-bound alpha-synuclein fibrils conformation 2|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN FIBRIL","7YNO|PiB-bound alpha-synuclein fibrils conformation 1|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7YNP|BF227-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7YNQ|PiB-bound alpha-synuclein fibrils conformation 2|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","7YNR|C05-03-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN FIBRIL","7YNS|SIL5-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7YNT|pFTAA-bound alpha-synuclein fibrils|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","8A4L|Lipidic alpha-synuclein fibril - polymorph L2A|ELECTRON MICROSCOPY|2.68|Homo sapiens|0|PROTEIN FIBRIL","8A9L|Cryo-EM structure of alpha-synuclein filaments from Parkinson's disease and dementia with Lewy bodies|ELECTRON MICROSCOPY|2.2|Homo sapiens|0|PROTEIN FIBRIL","8ADS|Lipidic alpha-synuclein fibril - polymorph L2B|ELECTRON MICROSCOPY|3.05|Homo sapiens|0|PROTEIN FIBRIL","8ADU|Lipidic alpha-synuclein fibril - polymorph L1A|ELECTRON MICROSCOPY|3.24|Homo sapiens|0|PROTEIN FIBRIL","8ADV|Lipidic alpha-synuclein fibril - polymorph L1B|ELECTRON MICROSCOPY|2.98|Homo sapiens|0|PROTEIN FIBRIL","8ADW|Lipidic alpha-synuclein fibril - polymorph L1C|ELECTRON MICROSCOPY|2.95|Homo sapiens|0|PROTEIN FIBRIL","8AEX|Lipidic alpha-synuclein fibril - polymorph L3A|ELECTRON MICROSCOPY|2.76|Homo sapiens|0|PROTEIN FIBRIL","8B9V|Crystal structure of Lu AF82422 in complex with alpha-synuclein 110-120|X-RAY DIFFRACTION|2.16|Homo sapiens; SYNTHETIC CONSTRUCT|0|PROTEIN BINDING","8BQV|Cryo-EM structure of alpha-synuclein singlet filament from Juvenile-onset synucleinopathy|ELECTRON MICROSCOPY|2.0|Homo sapiens|0|PROTEIN FIBRIL","8BQW|Cryo-EM structure of alpha-synuclein filaments doublet from Juvenile-onset synucleinopathy|ELECTRON MICROSCOPY|2.3|Homo sapiens|0|PROTEIN FIBRIL","8CE7|Type1 alpha-synuclein filament assembled in vitro by wild-type and mutant (7 residues insertion) protein|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN FIBRIL","8CEB|Type2 alpha-synuclein filament assembled in vitro by wild-type and mutant (7 residues insertion) protein|ELECTRON MICROSCOPY|2.8|Homo sapiens|0|PROTEIN FIBRIL","8CYR|Alpha-synuclein fibril from spontaneous control|ELECTRON MICROSCOPY|4.2|Homo sapiens|0|PROTEIN FIBRIL","8CYS|CryoEM structures of amplified alpha-synuclein fibril class B type II with extended core from DLB case I|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","8CYT|CryoEM structures of amplified alpha-synuclein fibril class A type I with extended core from DLB case I|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","8CYV|CryoEM structures of amplified alpha-synuclein fibril class B mixed type I/II with extended core from DLB case II|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","8CYW|CryoEM structures of amplified alpha-synuclein fibril class B type I with compact core from DLB case III|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL"]},{"input":"Q5S007","source":"Q5S007|Leucine-rich repeat serine/threonine-protein kinase 2","targets":["2ZEJ|Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase|X-RAY DIFFRACTION|2|Homo sapiens|0|TRANSFERASE","3D6T|Structure of the ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2 reveals a dimeric GTPase|X-RAY DIFFRACTION|2.43|Homo sapiens|0|TRANSFERASE","5MY9|Crystal structure of human 14-3-3 sigma in complex with LRRK2 peptide pS935|X-RAY DIFFRACTION|1.327|Homo sapiens; SYNTHETIC CONSTRUCT|0|TRANSFERASE","5MYC|Crystal structure of human 14-3-3 sigma in complex with LRRK2 peptide pS910|X-RAY DIFFRACTION|1.459|Homo sapiens; SYNTHETIC CONSTRUCT|0|TRANSFERASE","6DLO|Crystal structure of LRRK2 WD40 domain dimer|X-RAY DIFFRACTION|2.7|Homo sapiens|0|CYTOSOLIC PROTEIN","6DLP|Crystal structure of LRRK2 WD40 domain dimer|X-RAY DIFFRACTION|4|Homo sapiens|0|CYTOSOLIC PROTEIN","6OJE|Dimeric structure of LRRK2 GTPase domain|X-RAY DIFFRACTION|1.95|Homo sapiens|0|HYDROLASE","6OJF|Dimeric structure of LRRK2 GTPase domain|X-RAY DIFFRACTION|1.6|Homo sapiens|0|HYDROLASE","6VNO|Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|SIGNALING PROTEIN","6VP6|Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)|ELECTRON MICROSCOPY|3.47|Homo sapiens|0|SIGNALING PROTEIN","6VP7|Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|SIGNALING PROTEIN","6VP8|Cryo-EM structure of the C-terminal half of the Parkinson's Disease-linked protein Leucine Rich Repeat Kinase 2 (LRRK2)|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|SIGNALING PROTEIN","6XAF|1.9A crystal structure of the GTPase domain of Parkinson's disease-associated protein LRRK2 carrying R1398H|X-RAY DIFFRACTION|1.968|Homo sapiens|0|HYDROLASE","6XR4|Integrative in situ structure of Parkinsons disease-linked human LRRK2|ELECTRON MICROSCOPY|14.0|Homo sapiens|0|SIGNALING PROTEIN, TRANSFERASE","7LHT|Structure of the LRRK2 dimer|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|TRANSFERASE, HYDROLASE","7LHW|Structure of the LRRK2 monomer|ELECTRON MICROSCOPY|3.7|Homo sapiens|0|TRANSFERASE, HYDROLASE","7LI3|Structure of the LRRK2 G2019S mutant|ELECTRON MICROSCOPY|3.8|Homo sapiens|0|TRANSFERASE, HYDROLASE","7LI4|Structure of LRRK2 after symmetry expansion|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|TRANSFERASE, HYDROLASE","7THY|Structure of Leucine Rich Repeat Kinase 2's ROC domain interacting with the microtubule facing the minus end|ELECTRON MICROSCOPY|5.2|Homo sapiens|0|CYTOSOLIC PROTEIN","7THZ|Structure of Leucine Rich Repeat Kinase 2's ROC domain interacting with the microtubule facing the plus end|ELECTRON MICROSCOPY|5.0|Homo sapiens|0|CYTOSOLIC PROTEIN","8FO2|Cryo-EM structure of Rab29-LRRK2 complex in the LRRK2 monomer state|ELECTRON MICROSCOPY|4.13|Homo sapiens|0|HYDROLASE","8FO7|Cryo-EM structure of LRRK2 bound to type I inhibitor LRRK2-IN-1|ELECTRON MICROSCOPY|3.52|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","8FO8|Cryo-EM structure of Rab29-LRRK2 complex in the LRRK2 dimer state|ELECTRON MICROSCOPY|3.88|Homo sapiens|0|HYDROLASE","8FO9|Cryo-EM structure of Rab29-LRRK2 complex in the LRRK2 tetramer state|ELECTRON MICROSCOPY|3.48|Homo sapiens|0|HYDROLASE","8SMC|Cryo-EM structure of LRRK2 bound with type-I inhibitor DNL201|ELECTRON MICROSCOPY|4.02|Homo sapiens|0|HYDROLASE","8TXZ|Structure of C-terminal LRRK2 bound to MLi-2|ELECTRON MICROSCOPY|3.05|Homo sapiens|0|PROTEIN BINDING","8TYQ|Structure of the C-terminal half of LRRK2 bound to GZD-824 (G2019S mutant)|ELECTRON MICROSCOPY|2.99|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8TZB|Structure of the C-terminal half of LRRK2 bound to GZD-824 (I2020T mutant)|ELECTRON MICROSCOPY|3.1|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8TZC|Structure of C-terminal LRRK2 bound to MLi-2 (G2019S mutant)|ELECTRON MICROSCOPY|2.7|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8TZE|Structure of C-terminal half of LRRK2 bound to GZD-824|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN BINDING","8TZF|Structure of full length LRRK2 bound to GZD-824 (I2020T mutant)|ELECTRON MICROSCOPY|3.4|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8TZG|Structure of C-terminal LRRK2 bound to MLi-2 (I2020T mutant)|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN BINDING","8TZH|Structure of full-length LRRK2 bound to MLi-2 (I2020T mutant)|ELECTRON MICROSCOPY|3.9|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8U1B|C-terminal LRRK2 bound to E11 DARPin|ELECTRON MICROSCOPY|3.7|Homo sapiens; synthetic construct|0|PROTEIN BINDING","8U7H|Cryo-EM structure of LRRK2 bound to type I inhibitor GNE-7915|ELECTRON MICROSCOPY|3.8|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","8U7L|Cryo-EM structure of LRRK2 bound to type II inhibitor GZD824|ELECTRON MICROSCOPY|3.6|Homo sapiens|0|HYDROLASE","8U8A|Cryo-EM structure of LRRK2 bound to type II inhibitor ponatinib|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","8U8B|Cryo-EM structure of LRRK2 bound to type II inhibitor rebastinib|ELECTRON MICROSCOPY|3.7|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","8VH4|Cryo-EM structure of Rab12-LRRK2 complex in the LRRK2 monomer state|ELECTRON MICROSCOPY|4.1|Homo sapiens|0|HYDROLASE","8VH5|Cryo-EM structure of Rab12-LRRK2 complex in the LRRK2 dimer state|ELECTRON MICROSCOPY|4.0|Homo sapiens|0|HYDROLASE","9C76|LRRK2 Roc domain RP (Ras-pocket) complexed to Divarasib|X-RAY DIFFRACTION|2.3|Homo sapiens|0|SIGNALING PROTEIN","9CHO|Autoinhibited full-length LRRK2(I2020T) on microtubules with MLi-2|ELECTRON MICROSCOPY|7.8|Homo sapiens|0|PROTEIN BINDING","9CI3|Structure of the LRRK2/14-3-3 complex|ELECTRON MICROSCOPY|3.96|Homo sapiens|0|TRANSFERASE/SIGNALING PROTEIN","9DMI|Structure of the C-terminal half of LRRK2 bound to RN277 (Type-II inhibitor)|ELECTRON MICROSCOPY|3.35|Homo sapiens; synthetic construct|0|PROTEIN BINDING"]},{"input":"P04062","source":"P04062|Lysosomal acid glucosylceramidase","targets":["1OGS|human acid-beta-glucosidase|X-RAY DIFFRACTION|2|Homo sapiens|0|HYDROLASE","1Y7V|X-ray structure of human acid-beta-glucosidase covalently bound to conduritol B epoxide|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE","2F61|Crystal structure of partially deglycosylated acid beta-glucosidase|X-RAY DIFFRACTION|2.5|Homo sapiens|0|HYDROLASE","2J25|Partially deglycosylated glucoceramidase|X-RAY DIFFRACTION|2.9|HOMO SAPIENS|0|HYDROLASE","2NSX|Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease|X-RAY DIFFRACTION|2.11|Homo sapiens|0|HYDROLASE","2NT0|Acid-beta-glucosidase low pH, glycerol bound|X-RAY DIFFRACTION|1.79|Homo sapiens|0|HYDROLASE","2NT1|Structure of acid-beta-glucosidase at neutral pH|X-RAY DIFFRACTION|2.3|Homo sapiens|0|HYDROLASE","2V3D|acid-beta-glucosidase with N-butyl-deoxynojirimycin|X-RAY DIFFRACTION|1.96|HOMO SAPIENS|0|HYDROLASE","2V3E|acid-beta-glucosidase with N-nonyl-deoxynojirimycin|X-RAY DIFFRACTION|2|HOMO SAPIENS|0|HYDROLASE","2V3F|acid-beta-glucosidase produced in carrot|X-RAY DIFFRACTION|1.95|HOMO SAPIENS|0|HYDROLASE","2VT0|X-ray structure of a conjugate with conduritol-beta-epoxide of acid-beta-glucosidase overexpressed in cultured plant cells|X-RAY DIFFRACTION|2.15|HOMO SAPIENS|0|HYDROLASE","2WCG|X-ray structure of acid-beta-glucosidase with N-octyl(cyclic guanidine)-nojirimycin in the active site|X-RAY DIFFRACTION|2.3|HOMO SAPIENS|0|HYDROLASE","2WKL|Velaglucerase alfa|X-RAY DIFFRACTION|2.7|HOMO SAPIENS|0|HYDROLASE","2XWD|X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6O-(N'-(N-OCTYL)IMINO)NOJIRIMYCIN IN THE ACTIVE SITE|X-RAY DIFFRACTION|2.66|HOMO SAPIENS|0|HYDROLASE","2XWE|X-RAY STRUCTURE OF ACID-BETA-GLUCOSIDASE WITH 5N,6S-(N'-(N-OCTYL)IMINO)-6-THIONOJIRIMYCIN IN THE ACTIVE SITE|X-RAY DIFFRACTION|2.31|HOMO SAPIENS|0|HYDROLASE","3GXD|Crystal structure of Apo acid-beta-glucosidase pH 4.5|X-RAY DIFFRACTION|2.5|Homo sapiens|0|HYDROLASE","3GXF|Crystal structure of acid-beta-glucosidase with isofagomine at neutral pH|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE","3GXI|Crystal structure of acid-beta-glucosidase at pH 5.5|X-RAY DIFFRACTION|1.84|Homo sapiens|0|HYDROLASE","3GXM|Crystal structure of acid-beta-glucosidase at pH 4.5, phosphate crystallization condition|X-RAY DIFFRACTION|2.2|Homo sapiens|0|HYDROLASE","3KE0|Crystal structure of N370S Glucocerebrosidase at acidic pH.|X-RAY DIFFRACTION|2.7|Homo sapiens|0|HYDROLASE","3KEH|Crystal Structure of N370S Glucocerebrosidase mutant at pH 7.4|X-RAY DIFFRACTION|2.8|Homo sapiens|0|HYDROLASE","3RIK|The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease|X-RAY DIFFRACTION|2.48|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","3RIL|The acid beta-glucosidase active site exhibits plasticity in binding 3,4,5,6-tetrahydroxyazepane-based inhibitors: implications for pharmacological chaperone design for gaucher disease|X-RAY DIFFRACTION|2.4|Homo sapiens|0|HYDROLASE/HYDROLASE INHIBITOR","5LVX|Crystal structure of glucocerebrosidase with an inhibitory quinazoline modulator|X-RAY DIFFRACTION|2.2|Homo sapiens|0|HYDROLASE","6MOZ|Structure of acid-beta-glucosidase in complex with an aromatic pyrrolidine iminosugar inhibitor|X-RAY DIFFRACTION|2.1|Homo sapiens|0|HYDROLASE","6Q1N|Glucocerebrosidase in complex with pharmacological chaperone IMX8|X-RAY DIFFRACTION|2.526|Homo sapiens|0|HYDROLASE/INHIBITOR","6Q1P|Glucocerebrosidase in complex with pharmacological chaperone norIMX8|X-RAY DIFFRACTION|2.796|Homo sapiens|0|HYDROLASE/INHIBITOR","6Q6K|Crystal structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol activity based probe with Cy5 tag (ME569)|X-RAY DIFFRACTION|1.92|Homo sapiens|0|HYDROLASE","6Q6L|Crystal structure of recombinant human beta-glucocerebrosidase in complex with adamantyl-cyclophellitol inhibitor (ME656)|X-RAY DIFFRACTION|1.81|Homo sapiens|0|HYDROLASE","6Q6N|Crystal structure of recombinant human beta-glucocerebrosidase in complex with biphenyl-cyclophellitol inhibitor (ME655)|X-RAY DIFFRACTION|1.63|Homo sapiens|0|HYDROLASE","6T13|CRYSTAL STRUCTURE OF GLUCOCEREBROSIDASE IN COMPLEX WITH A PYRROLOPYRAZINE|X-RAY DIFFRACTION|1.85|Homo sapiens|0|HYDROLASE","6TJJ|Structure of Cerezyme at pH 4.6|X-RAY DIFFRACTION|1.59|Homo sapiens|0|HYDROLASE","6TJK|Crystal Structure of Recombinant GBA in Complex with Bis-Tris Propane.|X-RAY DIFFRACTION|1.56|Homo sapiens|0|HYDROLASE","6TJQ|Crystal Structure of Recombinant GBA in Complex with 2-Deoxy-2-fluoro-beta-D-glucopyranoside|X-RAY DIFFRACTION|1.41|Homo sapiens|0|HYDROLASE","6TN1|Unliganded Crystal Structure of Recombinant GBA|X-RAY DIFFRACTION|0.98|Homo sapiens|0|HYDROLASE","6YTP|Structure of recombinant human beta-glucocerebrosidase in complex with azide tagged cyclophellitol epoxide inhibitor|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6YTR|Structure of recombinant human beta-glucocerebrosidase in complex with cyclophellitol aziridine inhibitor|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6YUT|Structure of recombinant human beta-glucocerebrosidase in complex with N-acyl functionalised cyclophellitol aziridine|X-RAY DIFFRACTION|1.76|Homo sapiens|0|HYDROLASE","6YV3|Structure of recombinant human beta-glucocerebrosidase in complex with galacto-configured cyclophellitol aziridine inhibitor|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE","6Z39|Structure of recombinant human beta-glucocerebrosidase in complex with BODIPY functionalised epoxide activity based probe|X-RAY DIFFRACTION|1.7|Homo sapiens|0|HYDROLASE","6Z3I|Structure of recombinant beta-glucocerebrosidase in complex with bifunctional cyclophellitol aziridine activity based probe|X-RAY DIFFRACTION|1.8|Homo sapiens|0|HYDROLASE","7NWV|Structure of recombinant human beta-glucocerebrosidase in complex with BODIPY Tagged Cyclophellitol activity based probe|X-RAY DIFFRACTION|1.86|Homo sapiens|0|HYDROLASE","8AWK|Structure of recombinant human beta-glucocerebrosidase in complex with D-carbaxylosyl chloride|X-RAY DIFFRACTION|1.58|Homo sapiens|0|HYDROLASE","8AWR|Structure of recombinant human beta-glucocerebrosidase in complex with L-carbaxylosyl chloride|X-RAY DIFFRACTION|1.49|Homo sapiens|0|HYDROLASE","8AX3|Structure of recombinant human beta-glucocerebrosidase in complex with L-carbaxylosyl fluoride|X-RAY DIFFRACTION|1.59|Homo sapiens|0|HYDROLASE","8P3E|Crystal structure of glucocerebrosidase in complex with allosteric activator|X-RAY DIFFRACTION|1.75|Homo sapiens|0|HYDROLASE","8P41|Crystal structure of glucocerebrosidase in complex with allosteric activator|X-RAY DIFFRACTION|1.83|Homo sapiens|0|HYDROLASE","9ENA|Lysosomal glucocerebrosidase in complex with a stabilizing nanobody|X-RAY DIFFRACTION|1.7|Homo sapiens; Lama glama|0|HYDROLASE","9F9Z|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|2.279|Homo sapiens|0|LIPID BINDING PROTEIN","9FA3|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.36|Homo sapiens|0|LIPID BINDING PROTEIN","9FA6|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.49|Homo sapiens|0|LIPID BINDING PROTEIN","9FAD|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.8|Homo sapiens|0|LIPID BINDING PROTEIN","9FAL|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.39|Homo sapiens|0|LIPID BINDING PROTEIN","9FAY|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.4|Homo sapiens|0|LIPID BINDING PROTEIN","9FAZ|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.63|Homo sapiens|0|LIPID BINDING PROTEIN","9FB2|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.14|Homo sapiens|0|LIPID BINDING PROTEIN","9FDI|Gcase in complex with small molecule inhibitor 1|X-RAY DIFFRACTION|1.41|Homo sapiens|0|LIPID BINDING PROTEIN","9FJF|Lysosomal transporting complex of beta-glucocerebrosidase (GCase) and lysosomal integral membrane protein 2 (LIMP-2) with bound Pro-macrobodies (Combined focus map)|ELECTRON MICROSCOPY|3.7|Homo sapiens; synthetic construct|0|TRANSPORT PROTEIN"]},{"input":"P10636","source":"P10636|Microtubule-associated protein tau","targets":["1I8H|SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE|SOLUTION NMR|||0|MEMBRANE PROTEIN/ISOMERASE","22JY|P301L/S320F human tau filaments from mouse brain|ELECTRON MICROSCOPY|2.2|Homo sapiens|0|PROTEIN FIBRIL","2MZ7|Structure of Tau(267-312) bound to Microtubules|SOLUTION NMR|||0|PROTEIN BINDING","2ON9|Structure of an amyloid forming peptide VQIVYK from the repeat region of Tau|X-RAY DIFFRACTION|1.51||0|PROTEIN FIBRIL","3OVL|Structure of an amyloid forming peptide VQIVYK from the TAU protein in complex with orange G|X-RAY DIFFRACTION|1.81||0|PROTEIN FIBRIL","4E0M|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form I)|X-RAY DIFFRACTION|1.75||0|PROTEIN FIBRIL","4E0N|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form II)|X-RAY DIFFRACTION|1.65||0|PROTEIN FIBRIL","4E0O|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form III)|X-RAY DIFFRACTION|1.82||0|PROTEIN FIBRIL","4FL5|Crystal structure of human 14-3-3 sigma in complex with a Tau-protein peptide surrounding pS214|X-RAY DIFFRACTION|1.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","4GLR|Structure of the anti-ptau Fab (pT231/pS235_1) in complex with phosphoepitope pT231/pS235|X-RAY DIFFRACTION|1.9|Gallus gallus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4NP8|Structure of an amyloid forming peptide VQIVYK from the second repeat region of tau (alternate polymorph)|X-RAY DIFFRACTION|1.51||0|PROTEIN FIBRIL","4TQE|Structure of tau peptide in complex with Tau5 antibody Fab fragment|X-RAY DIFFRACTION|1.6|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4Y32|Crystal structure of C-terminal modified Tau peptide-hybrid 109B with 14-3-3sigma|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","4Y5I|Crystal structure of C-terminal modified Tau peptide-hybrid 126B with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","5BTV|Crystal structure of human 14-3-3 sigma in complex with a Tau-protein peptide surrounding pS324|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","5DMG|X-RAY STRUCTURE OF THE FAB FRAGMENT OF THE ANTI TAU ANTIBODY RB86 IN COMPLEX WITH THE PHOSPHORYLATED TAU PEPTIDE (416-430)|X-RAY DIFFRACTION|2.5|Oryctolagus cuniculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5E2V|Anti-TAU AT8 FAB with doubly phosphorylated TAU peptide|X-RAY DIFFRACTION|1.64|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5E2W|Anti-TAU AT8 FAB with triply phosphorylated TAU peptide|X-RAY DIFFRACTION|1.5|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5HF3|Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma|X-RAY DIFFRACTION|1.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","5K7N|MicroED structure of tau VQIVYK peptide at 1.1 A resolution|ELECTRON CRYSTALLOGRAPHY|1.1||0|PROTEIN FIBRIL","5MO3|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 8.5|X-RAY DIFFRACTION|1.69|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP1|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 7.5|X-RAY DIFFRACTION|3.1|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP3|Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5|X-RAY DIFFRACTION|2.75|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP5|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 6.5|X-RAY DIFFRACTION|2.31|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5N5A|Structure of Tau(254-290) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5N5B|Structure of Tau(292-319) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5NVB|Structure of Tau(254-268) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5O3L|Paired helical filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|STRUCTURAL PROTEIN","5O3O|Pronase-treated paired helical filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","5O3T|Straight filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","5V5B|KVQIINKKLD, Structure of the amyloid spine from microtubule associated protein tau Repeat 2|ELECTRON CRYSTALLOGRAPHY|1.5||0|STRUCTURAL PROTEIN","5V5C|VQIINK, Structure of the amyloid-spine from microtubule associated protein tau Repeat 2|ELECTRON CRYSTALLOGRAPHY|1.25||0|STRUCTURAL PROTEIN","5ZIA|Crystal structure of human anti-tau antibody CBTAU-24.1 in complex with its phosphorylated tau peptide|X-RAY DIFFRACTION|2.603|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5ZV3|Crystal structure of human anti-tau antibody CBTAU-28.1 in complex with its tau peptide|X-RAY DIFFRACTION|2.093|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6BB4|Fab/epitope complex of mouse monoclonal antibody C5.2 targeting a phospho-tau epitope.|X-RAY DIFFRACTION|2.099|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6CVJ|Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the microtubule|ELECTRON MICROSCOPY|3.2|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","6CVN|Model of synthetic tau (R2x4) bound to the microtubule|ELECTRON MICROSCOPY|3.9|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","6DC8|Fab/epitope complex of mouse monoclonal antibody 8B2 targeting a non-phosphorylated tau epitope.|X-RAY DIFFRACTION|1.799|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6DC9|Fab/epitope complex of human chimeric monoclonal antibody h4E6 targeting a phosphorylated tau epitope.|X-RAY DIFFRACTION|2.999|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6DCA|Fab/epitope complex of mouse monoclonal antibody 6B2 targeting a non-phosphorylated tau epitope.|X-RAY DIFFRACTION|2.599|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6FAU|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2e-I with 14-3-3sigma|X-RAY DIFFRACTION|1.25|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FAV|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-I with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FAW|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2c-I with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FBW|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-II with 14-3-3sigma|X-RAY DIFFRACTION|1.45|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FBY|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2b with 14-3-3sigma|X-RAY DIFFRACTION|1.5|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FI4|Crystal structure of C-terminal modified Tau peptide-hybrid 3.2e with 14-3-3sigma|X-RAY DIFFRACTION|2|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FI5|Crystal structure of C-terminal modified Tau peptide-hybrid 3.2d with 14-3-3sigma|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6GK7|Crystal structure of anti-tau antibody dmCBTAU-27.1, double mutant (S31Y, T100I) of CBTAU-27.1, in complex with Tau peptide A8119B (residues 299-318)|X-RAY DIFFRACTION|2.95|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6GK8|Crystal structure of anti-tau antibody dmCBTAU-28.1, double mutant (S32R, E35K) of CBTAU-28.1, in complex with Tau peptide A7731 (residues 52-71)|X-RAY DIFFRACTION|2.85|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6GX5|Narrow Pick Filament from Pick's disease brain|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6H06|FAB CBTAU-22.1 IN COMPLEX WITH TAU PEPTIDE V1088-5|X-RAY DIFFRACTION|2.63|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6HRE|Paired helical filament from sporadic Alzheimer's disease brain|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6HRF|Straight filament from sporadic Alzheimer's disease brain|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6LRA|The complex structure of PHF core domain peptide of tau and antibody's Fab domain.|X-RAY DIFFRACTION|1.9|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6N4P|RQEFEV, crystal structure of the N-terminal segment RQEFEV from protein tau|X-RAY DIFFRACTION|1.851||0|PROTEIN FIBRIL","6NK4|KVQIINKKL, crystal structure of a tau protein fragment|ELECTRON CRYSTALLOGRAPHY|1.994||0|STRUCTURAL PROTEIN","6NWP|Chronic traumatic encephalopathy Type I Tau filament|ELECTRON MICROSCOPY|2.3|Homo sapiens|0|PROTEIN FIBRIL","6NWQ|Chronic traumatic encephalopathy Type II Tau filament|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","6ODG|SVQIVY, Crystal Structure of a tau protein fragment|X-RAY DIFFRACTION|1||0|PROTEIN FIBRIL","6PXR|Anti-TAU BIIB092 FAB with TAU peptide|X-RAY DIFFRACTION|1.556|Homo sapiens; Mus musculus|0|IMMUNE SYSTEM","6QJH|Cryo-EM structure of heparin-induced 2N4R tau snake filaments|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6QJM|Cryo-EM structure of heparin-induced 2N4R tau twister filaments|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6QJP|Cryo-EM structure of heparin-induced 2N4R tau jagged filaments|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","6QJQ|Cryo-EM structure of heparin-induced 2N3R tau filaments|ELECTRON MICROSCOPY|3.7|Homo sapiens|0|PROTEIN FIBRIL","6TJO|Cryo-EM structure of TypeI tau filaments extracted from the brains of individuals with Corticobasal degeneration|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6TJX|Cryo-EM structure of TypeII tau filaments extracted from the brains of individuals with Corticobasal degeneration|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","6VH7|Doublet Tau Fibril from Corticobasal Degeneration Human Brain Tissue|ELECTRON MICROSCOPY|3.8|Homo sapiens|0|PROTEIN FIBRIL","6VHA|Singlet Tau Fibril from Corticobasal Degeneration Human Brain Tissue|ELECTRON MICROSCOPY|4.3|Homo sapiens|0|PROTEIN FIBRIL","6VHL|Paired Helical Filament from Alzheimer's Disease Human Brain Tissue|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6VI3|Straight Filament from Alzheimer's Disease Human Brain Tissue|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6XLI|CRYSTAL STRUCTURE OF ANTI-TAU ANTIBODY PT3 Fab+pT212/pT217-TAU PEPTIDE|X-RAY DIFFRACTION|2|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7EYC|Crystal structure of Tau and acetylated tau peptide antigen|X-RAY DIFFRACTION|2.49|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7KQK|anti-pTau C21-ABS Fab in complex with pTau peptide|X-RAY DIFFRACTION|2.6|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7MKF|Paired helical tau filament extracted from PrP-CAA Patient brain tissue \\| tau filament \\| PHF Tau|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7MKG|Straight tau filament extracted from PrP-CAA Patient brain tissue \\| tau filament \\| SF Tau|ELECTRON MICROSCOPY|3.07|Homo sapiens|0|PROTEIN FIBRIL","7MKH|Paired helical tau filament extracted from GSS Patient brain tissue \\| tau filament from Gerstmann Straussler Scheinker disease \\| PHF Tau|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7NRQ|Paired helical filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.76|Homo sapiens|0|PROTEIN FIBRIL","7NRS|Conformation 1 of straight filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.68|Homo sapiens|0|PROTEIN FIBRIL","7NRT|Conformation 2 of straight filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.68|Homo sapiens|0|PROTEIN FIBRIL","7NRV|Paired helical filament from Alzheimer's disease with PET ligand APN-1607|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7NRX|Straight filament from Alzheimer's disease with PET ligand APN-1607|ELECTRON MICROSCOPY|3.55|Homo sapiens|0|PROTEIN FIBRIL","7P65|Progressive supranuclear palsy tau filament|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN FIBRIL","7P66|Globular glial tauopathy type 1 tau filament|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7P67|Globular glial tauopathy type 2 tau filament|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","7P68|Globular glial tauopathy type 3 tau filament|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN FIBRIL","7P6A|Limbic-predominant neuronal inclusion body 4R tauopathy type 1a tau filament|ELECTRON MICROSCOPY|1.9|Homo sapiens|0|PROTEIN FIBRIL","7P6B|Limbic-predominant neuronal inclusion body 4R tauopathy type 1b tau filament|ELECTRON MICROSCOPY|2.2|Homo sapiens|0|PROTEIN FIBRIL","7P6C|Limbic-predominant neuronal inclusion body 4R tauopathy type 2 tau filament|ELECTRON MICROSCOPY|2.5|Homo sapiens|0|PROTEIN FIBRIL","7P6D|Argyrophilic grain disease type 1 tau filament|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7P6E|Argyrophilic grain disease type 2 tau filament|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7PQC|tau-microtubule structural ensemble based on CryoEM data|ELECTRON MICROSCOPY|4.1|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","7PQP|tau-microtubule structural ensemble based on CryoEM data|ELECTRON MICROSCOPY|4.1|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","7QJV|In vitro assembled tau filaments into Quadruple Helical Filaments type 1 (2c)|ELECTRON MICROSCOPY|3.29|Homo sapiens|0|PROTEIN FIBRIL","7QJW|In vitro assembled tau filaments with structures like chronic traumatic encephalopathy type II (8a)|ELECTRON MICROSCOPY|2.81|Homo sapiens|0|PROTEIN FIBRIL","7QJX|In vitro assembled 297-394 tau filaments, 700 rpm (34b)|ELECTRON MICROSCOPY|2.99|Homo sapiens|0|PROTEIN FIBRIL","7QJY|In vitro assembled 266/297 - 391 tau filaments with LiCl (9a)|ELECTRON MICROSCOPY|3.14|Homo sapiens|0|PROTEIN FIBRIL","7QJZ|In vitro assembled 266/297 - 391 tau filaments with LiCl (9b)|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7QK1|In vitro assembled 297-394 tau filaments in PBS (35d)|ELECTRON MICROSCOPY|3.03|Homo sapiens|0|PROTEIN FIBRIL","7QK2|In vitro assembled 300-391 tau filaments in PBS (36a)|ELECTRON MICROSCOPY|2.61|Homo sapiens|0|PROTEIN FIBRIL","7QK3|In vitro assembled 258-391 tau filaments, 700 rpm (38a)|ELECTRON MICROSCOPY|2.44|Homo sapiens|0|PROTEIN FIBRIL"]},{"input":"O60260","source":"O60260|E3 ubiquitin-protein ligase parkin","targets":["1IYF|Solution structure of ubiquitin-like domain of human parkin|SOLUTION NMR||Homo sapiens|0|LIGASE","2JMO|IBR domain of Human Parkin|SOLUTION NMR||Homo sapiens|0|LIGASE","4BM9|Structure of the autoinhibited Parkin catalytic domain|X-RAY DIFFRACTION|2.25|HOMO SAPIENS|0|LIGASE","4I1F|Structure of Parkin-S223P E3 ligase|X-RAY DIFFRACTION|1.58|Homo sapiens|0|LIGASE","4I1H|Structure of Parkin E3 ligase|X-RAY DIFFRACTION|2|Homo sapiens|0|LIGASE","5C1Z|Parkin (UblR0RBR)|X-RAY DIFFRACTION|1.79|Homo sapiens|0|LIGASE","5C23|Parkin (S65DUblR0RBR)|X-RAY DIFFRACTION|2.37|Homo sapiens|0|LIGASE","5C9V|Structure of human Parkin G319A|X-RAY DIFFRACTION|2.35|Homo sapiens|0|SIGNALING PROTEIN","5N2W|WT-Parkin and pUB complex|X-RAY DIFFRACTION|2.68|Homo sapiens|0|LIGASE","5N38|S65DParkin and pUB complex|X-RAY DIFFRACTION|2.6|Homo sapiens|0|LIGASE","5TR5|Solution structure of Serine 65 phosphorylated UBL domain from parkin|SOLUTION NMR||Homo sapiens|0|LIGASE","6GLC|Structure of phospho-Parkin bound to phospho-ubiquitin|X-RAY DIFFRACTION|1.8|Homo sapiens|0|LIGASE","6HUE|ParkinS65N|X-RAY DIFFRACTION|2.85|Homo sapiens|0|LIGASE","6N13|UbcH7-Ub Complex with R0RBR Parkin and phosphoubiquitin|SOLUTION NMR||Homo sapiens|0|LIGASE","8IK6|pUbl depleted Parkin complex with pUbiquitin|X-RAY DIFFRACTION|3.3|Homo sapiens|0|LIGASE","8IKM|Trans complex of phospho parkin|X-RAY DIFFRACTION|1.92|Homo sapiens|0|LIGASE","8IKT|Ternary trans-complex of phospho-parkin with cis ACT and pUb|X-RAY DIFFRACTION|2.6|Homo sapiens|0|LIGASE","8IKV|pUbl depleted phospho-Parkin(K211N,R163D) in complex with pUb|X-RAY DIFFRACTION|2.35|Homo sapiens|0|LIGASE","8JWV|Untethered R0RBR|X-RAY DIFFRACTION|2.9|Homo sapiens|0|LIGASE","8WZN|ParkinK211N in complex with phospho NEDD8|X-RAY DIFFRACTION|1.8|Homo sapiens|0|LIGASE","8WZO|Parkin in complex with phospho NEDD8|X-RAY DIFFRACTION|2.25|Homo sapiens|0|LIGASE"]}]}