Structure of PDB 5nge Chain A

Receptor sequence
>5ngeA (length=337) Species: 9606 (Homo sapiens) [Search protein sequence]
GYVGLKNQGATCYMNSLLQTLFFTNQLRKAVYMMPTEGDDSSKSVPLALQ
RVFYELQHSDKPVGTKKLTKSFGWETLDSFMQHDVQELCRVLLDNVENKM
KGTCVEGTIPKLFRGKMVSYIQCKEVDYRSDRREDYYDIQLSIKGKKNIF
ESFVDYVAVEQLDGDNKYDAGEHGLQEAEKGVKFLTLPPVLHLQLMRFMY
DPQTDQNIKINDRFEFPEQLPLDEFLQKTDPKDPANYILHAVLVHSGDNH
GGHYVVYLNPKGDGKWCKFDDDVVSRCTKEEAIEHNYGGHCTNAYMLVYI
RESKLSEVLQAVTDHDIPQQLVERLQEEKRIEAQKRK
3D structure
PDB5nge Molecular basis of USP7 inhibition by selective small-molecule inhibitors.
ChainA
Resolution2.35 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) N7 C12 H253 D270
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 8WK A Y224 D295 Q297 Q351 L406 M407 R408 F409 H456 D459 N460 H461 Y465 Y514 Y13 D84 Q86 Q140 L195 M196 R197 F198 H245 D248 N249 H250 Y254 Y295 MOAD: Kd=65nM
PDBbind-CN: -logKd/Ki=7.19,Kd=65nM
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:5nge, PDBe:5nge, PDBj:5nge
PDBsum5nge
PubMed29045389
UniProtQ93009|UBP7_HUMAN Ubiquitin carboxyl-terminal hydrolase 7 (Gene Name=USP7)

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