Structure of PDB 5vsb Chain A

Receptor sequence
>5vsbA (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
TGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLAL
QRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENK
MKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNI
FESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFM
YDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDN
HGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGCTNAYMLVYI
RESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQK
3D structure
PDB5vsb Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) N218 C223 H464 D481
Catalytic site (residue number reindexed from 1) N8 C13 H254 D271
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
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 9QA A Y224 D295 Q297 L406 M407 R408 F409 K420 H456 H461 Y465 Y514 Y14 D85 Q87 L196 M197 R198 F199 K210 H246 H251 Y255 Y295 MOAD: Kd=7.614uM
PDBbind-CN: -logKd/Ki=5.12,Kd=7.614uM
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
Biological Process
GO:0016579 protein deubiquitination

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Molecular Function
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Biological Process
External links
PDB RCSB:5vsb, PDBe:5vsb, PDBj:5vsb
PDBsum5vsb
PubMed29056421
UniProtQ93009|UBP7_HUMAN Ubiquitin carboxyl-terminal hydrolase 7 (Gene Name=USP7)

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