Structure of PDB 5y3o Chain A

Receptor sequence
>5y3oA (length=433) Species: 9606 (Homo sapiens) [Search protein sequence]
EPLHSIISSTESVQGSTSKHEFQAETKKLLDIVARSLYSEKEVFIRELIS
NASDALEKLRHKLVSDGQALPEMEIHLQTNAEKGTITIQDTGIGMTQEEL
VSFGVGFYSAFMVADRVEVYSRSAAPGSLGYQWLSDGSGVFEIAEASGVR
TGTKIIIHLKSDCKEFSSEARVRDVVTKYSNFVSFPLYLNGRRMNTLQAI
WMMDPKDVREWQHEEFYRYVAQAHDKPRYTLHYKTDAPLNIRSIFYVPDM
KPSVALYSRKVLIQTKATDILPKWLRFIRGVVDSEDIPSALIRKLRDVLQ
QRLIKFFIDQSKKDAEKYAKFFEDYGLFMREGIVTATEQEVKEDIAKLLR
YESSALPSGQLTSLSEYASRMRAGTRNIYYLCAPNRHLAEHSPYYEAMKK
KDTEVLFCFEQFDELTLLHLREFDKKKLISVET
3D structure
PDB5y3o Paralog Specificity Determines Subcellular Distribution, Action Mechanism, and Anticancer Activity of TRAP1 Inhibitors.
ChainA
Resolution2.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 8M9 A D158 I161 G162 M163 F201 F205 V217 W231 T251 D90 I93 G94 M95 F103 F107 V119 W133 T153 PDBbind-CN: -logKd/Ki=6.86,IC50=0.138uM
BindingDB: IC50=138nM
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:5y3o, PDBe:5y3o, PDBj:5y3o
PDBsum5y3o
PubMed28816449
UniProtQ12931|TRAP1_HUMAN Heat shock protein 75 kDa, mitochondrial (Gene Name=TRAP1)

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