Structure of PDB 8a9j Chain D

Receptor sequence
>8a9jD (length=330) Species: 9606 (Homo sapiens) [Search protein sequence]
NLLPFVGLNNLGNTSYLNSILQVLYFCPGFKSGVKHLFNIISRKKEASYE
LICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEG
YLQHDAQEVLQCILGNIQETCQLLKKEEGFELVEKLFQGQLVLRTRCLEC
ESLTERREDFQDISVPVQEDMKTLRWAISQFASVERIVGEDKYFCENCHH
YTEAERSLLFDKMPEVITIHLKCFAASGLSKINTPLLTPLKLSLEEWSTK
PTNDSYGLFAVVMHSGITISSGHYTASVKVTVQSLKEYEGKWLLFDDSEV
KVTEEKDFLNSLSPSTSPTSTPYLLFYKKL
3D structure
PDB8a9j Cryo-EM reveals a mechanism of USP1 inhibition through a cryptic binding site.
ChainD
Resolution2.8 Å
3D
structure
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Enzymatic activity
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 ZN D C440 C443 C506 C509 C147 C150 C195 C198
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
GO:0004843 cysteine-type deubiquitinase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0001501 skeletal system development
GO:0006281 DNA repair
GO:0006282 regulation of DNA repair
GO:0006508 proteolysis
GO:0009411 response to UV
GO:0016579 protein deubiquitination
GO:0035520 monoubiquitinated protein deubiquitination
GO:0046427 positive regulation of receptor signaling pathway via JAK-STAT
GO:1904333 positive regulation of error-prone translesion synthesis
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:8a9j, PDBe:8a9j, PDBj:8a9j
PDBsum8a9j
PubMed36170365
UniProtO94782|UBP1_HUMAN Ubiquitin carboxyl-terminal hydrolase 1 (Gene Name=USP1)

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