{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":1,"total":44,"mapped":1},"pagination":{"has_next":false},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"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"]}]}