Structure of PDB 5vs6 Chain B

Receptor sequence
>5vs6B (length=337) Species: 9606 (Homo sapiens) [Search protein sequence]
KHTGYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPL
ALQRVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVE
NKMKGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKK
NIFESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMR
FMYDPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSG
DNHGGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGCTNAYMLV
YIRESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQK
3D structure
PDB5vs6 Structure-Guided Development of a Potent and Selective Non-covalent Active-Site Inhibitor of USP7.
ChainB
Resolution2.27 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) N10 C15 H256 D273
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 9QD B Y224 D295 Q297 L406 M407 R408 F409 K420 H456 N460 H461 Y465 Y514 Y16 D87 Q89 L198 M199 R200 F201 K212 H248 N252 H253 Y257 Y297 MOAD: Kd=104nM
BindingDB: IC50=90nM
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:5vs6, PDBe:5vs6, PDBj:5vs6
PDBsum5vs6
PubMed29056421
UniProtQ93009|UBP7_HUMAN Ubiquitin carboxyl-terminal hydrolase 7 (Gene Name=USP7)

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