Structure of PDB 5k1b Chain A

Receptor sequence
>5k1bA (length=264) Species: 9606 (Homo sapiens) [Search protein sequence]
GLVNFGNTCYCNSVLQALYFCRPFREKVLAYKSQESLLTCLADLFHSIAT
QVIPPKKFITRLRKENELFDNYMQQDAHEFLNYLLNTIADILQEEPTWVH
EIFQGTLTNETRCLTCETISSKDEDFLDLSVDVSITHCLRGFSNTETLCS
EYKYYCEECRSKQEAHKRMKVKKLPMILALHLKRFSYRVVFPLELRLFPD
RMYDLVAVVVHCGSGPNRGHYIAIVKSHWLLFDDDIVEKIDAQAIEEFYK
NSESGYILFYQSRD
3D structure
PDB5k1b Allosteric Activation of Ubiquitin-Specific Proteases by beta-Propeller Proteins UAF1 and WDR20.
ChainA
Resolution3.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) G40 G45 H317 D332
Catalytic site (residue number reindexed from 1) G1 G6 H220 D233
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 A C186 C233 C236 C113 C156 C159
Gene Ontology
Molecular Function
GO:0004197 cysteine-type endopeptidase activity
GO:0004843 cysteine-type deubiquitinase activity
GO:0005515 protein binding
GO:0008234 cysteine-type peptidase activity
GO:0046872 metal ion binding
GO:0101005 deubiquitinase activity
Biological Process
GO:0006508 proteolysis
GO:0016579 protein deubiquitination
Cellular Component
GO:0005575 cellular_component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5k1b, PDBe:5k1b, PDBj:5k1b
PDBsum5k1b
PubMed27373336
UniProtO75317|UBP12_HUMAN Ubiquitin carboxyl-terminal hydrolase 12 (Gene Name=USP12)

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