{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":1,"total":31,"mapped":1},"pagination":{"has_next":false},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"P42858","source":"P42858|Huntingtin","targets":["2LD0|Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFE|SOLUTION NMR|||0|LIPID BINDING PROTEIN","2LD2|Solution structure of the N-terminal domain of huntingtin (htt17) in presence of DPC micelles|SOLUTION NMR|||0|LIPID BINDING PROTEIN","3IO4|Huntingtin amino-terminal region with 17 Gln residues - Crystal C90|X-RAY DIFFRACTION|3.63|Escherichia coli O157:H7; Homo sapiens|0|SIGNALING PROTEIN","3IO6|Huntingtin amino-terminal region with 17 Gln residues - crystal C92-a|X-RAY DIFFRACTION|3.7|Escherichia coli K-12, Homo sapiens|0|SIGNALING PROTEIN","3IOR|Huntingtin amino-terminal region with 17 Gln residues - crystal C95|X-RAY DIFFRACTION|3.6|Escherichia coli K-12, Homo sapiens|0|SIGNALING PROTEIN","3IOT|Huntingtin amino-terminal region with 17 Gln residues - crystal C92-b|X-RAY DIFFRACTION|3.5|Escherichia coli (strain K12); Homo sapiens|0|SIGNALING PROTEIN","3IOU|Huntingtin amino-terminal region with 17 Gln residues - crystal C94|X-RAY DIFFRACTION|3.7|Escherichia coli; Homo sapiens|0|SIGNALING PROTEIN","3IOV|Huntingtin amino-terminal region with 17 Gln residues - crystal C99|X-RAY DIFFRACTION|3.7|Escherichia coli (strain K12); Homo sapiens|0|SIGNALING PROTEIN","3IOW|Huntingtin amino-terminal region with 17 Gln residues - crystal C99-Hg|X-RAY DIFFRACTION|3.5|Escherichia coli (strain K12); Homo sapiens|0|SIGNALING PROTEIN","3LRH|Structure of anti-huntingtin VL domain in complex with huntingtin peptide|X-RAY DIFFRACTION|2.6|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4FE8|Crystal Structure of Htt36Q3H-EX1-X1-C1(Alpha)|X-RAY DIFFRACTION|3|Escherichia coli (strain K12); Homo sapiens|0|SIGNALING PROTEIN","4FEB|Crystal Structure of Htt36Q3H-EX1-X1-C2(Beta)|X-RAY DIFFRACTION|2.8|Escherichia coli O157:H7; Homo sapiens|0|SIGNALING PROTEIN","4FEC|Crystal Structure of Htt36Q3H|X-RAY DIFFRACTION|3|Escherichia coli (strain K12); Homo sapiens|0|SIGNALING PROTEIN","4FED|Crystal Structure of Htt36Q3H|X-RAY DIFFRACTION|2.807|Escherichia coli; Homo sapiens|0|SIGNALING PROTEIN","4RAV|Crystal structure of scFvC4 in complex with the first 17 AA of huntingtin|X-RAY DIFFRACTION|2.5|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM/Apoptosis","6EZ8|Human Huntingtin-HAP40 complex structure|ELECTRON MICROSCOPY|4.0|Homo sapiens|0|PROTEIN BINDING","6N8C|Structure of the Huntingtin tetramer/dimer mixture determined by paramagnetic NMR|SOLUTION NMR||Homo sapiens|0|UNKNOWN FUNCTION","6RMH|The Rigid-body refined model of the normal Huntingtin.|ELECTRON MICROSCOPY|9.6|Homo sapiens|0|PROTEIN BINDING","6X9O|High resolution cryoEM structure of huntingtin in complex with HAP40|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|PROTEIN BINDING","6YEJ|Cryo-EM structure of the Full-length disease type human Huntingtin|ELECTRON MICROSCOPY|18.2|Homo sapiens|0|STRUCTURAL PROTEIN","7DXJ|Human 46QHuntingtin-HAP40 complex structure|ELECTRON MICROSCOPY|3.6|Homo sapiens; synthetic construct|0|STRUCTURAL PROTEIN","7DXK|Human 128QHuntingtin-HAP40 complex structure|ELECTRON MICROSCOPY|4.1|Homo sapiens; synthetic construct|0|STRUCTURAL PROTEIN","8R2O|Huntingtin-Q17, 1-66, N-MBP fusion|X-RAY DIFFRACTION|3.23|Homo sapiens|0|UNKNOWN FUNCTION","8SAH|Huntingtin C-HEAT domain in complex with HAP40|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN BINDING","8VLX|HTT in complex with HAP40 and a small molecule.|ELECTRON MICROSCOPY|2.6|Homo sapiens|0|UNKNOWN FUNCTION","8W15|HTT in complex with HAP40 in the apo state.|ELECTRON MICROSCOPY|2.72|Homo sapiens|0|UNKNOWN FUNCTION","8YAE|Cryo-ET structure of huntingtin actin complex|ELECTRON MICROSCOPY|10.08|Homo sapiens; Oryctolagus cuniculus|0|CYTOSOLIC PROTEIN/CONTRACTILE PROTEIN","8YAO|Cryo-ET structure of huntingtin actin dimer complex|ELECTRON MICROSCOPY|20.8|Homo sapiens; Oryctolagus cuniculus|0|CYTOSOLIC PROTEIN/CONTRACTILE PROTEIN","9PMW|Structure of HTTQ23-HAP40 complex bound to macrocycles HHL1, HD4 and HL2|ELECTRON MICROSCOPY|2.1|Homo sapiens; SYNTHETIC CONSTRUCT|0|PEPTIDE BINDING PROTEIN","9PN0|Structure of HTTQ23-HAP40 complex bound to macrocycles HHD3, HD4 and HL2|ELECTRON MICROSCOPY|2.3|Homo sapiens; SYNTHETIC CONSTRUCT|0|PEPTIDE BINDING PROTEIN","9YR6|Structure of HTTQ23-HAP40 complex bound to a small molecule ligand|ELECTRON MICROSCOPY|2.3|Homo sapiens|0|PEPTIDE BINDING PROTEIN"]}]}