Structure of PDB 5vsk Chain A

Receptor sequence
>5vskA (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
KKHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVP
LALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNV
ENKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGK
KNIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLM
RFMNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNHGGH
YVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHCTNAYMLVYIRES
KLSEVLQAVTDHDIPQQLVERLQEEKRIEA
3D structure
PDB5vsk Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7.
ChainA
Resolution3.33 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) N11 C16 H250 D267
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 9HS A Y224 D295 V296 M407 R408 F409 K420 H456 Y465 Y17 D88 V89 M200 R201 F202 K206 H242 Y251 PDBbind-CN: -logKd/Ki=5.74,Kd=1.838uM
BS02 ZN A C300 D349 H403 C93 D142 H196
BS03 ZN A H464 D481 H250 D267
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:5vsk, PDBe:5vsk, PDBj:5vsk
PDBsum5vsk
PubMed29056421
UniProtQ93009|UBP7_HUMAN Ubiquitin carboxyl-terminal hydrolase 7 (Gene Name=USP7)

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