Structure of PDB 7ay0 Chain D Binding Site BS01

Receptor Information
>7ay0 Chain D (length=285) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
NNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIIYELICSLQSLIISVEQL
QASFLLNPTQPRRLLNTLRELNPMDAQEVLQCILGNIQETCQLLKKVEKL
FQGQLVLRTRCLECESLTERREDFQDISVPVQEDEEMKTLRWAISQFASV
ERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEGGLS
KINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKV
WLLFDDSEVKVTEEKDFLNSLSPTSTPYLLFYKKL
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain7ay0 Chain D Residue 1000 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB7ay0 Structural basis of FANCD2 deubiquitination by USP1-UAF1.
Resolution3.6 Å
Binding residue
(original residue number in PDB)		C440 C443 C506 C509
Binding residue
(residue number reindexed from 1)		C111 C114 C161 C164
Annotation score4
Enzymatic activity
Enzyme Commision number 3.4.19.12: ubiquitinyl hydrolase 1.
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
GO:0004843 cysteine-type deubiquitinase activity
Biological Process
GO:0006282 regulation of DNA repair
GO:0016579 protein deubiquitination

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Molecular Function
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Biological Process
External links
PDB RCSB:7ay0, PDBe:7ay0, PDBj:7ay0
PDBsum7ay0
PubMed33795880
UniProtO94782|UBP1_HUMAN Ubiquitin carboxyl-terminal hydrolase 1 (Gene Name=USP1)

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