Structure of PDB 3jck Chain G

Receptor sequence
>3jckG (length=257) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
KETVYISSIALLKMLKHGRAGVPMEVMGLMLGEFVDDYTVNVVDVFAMPQ
SGTGVSVEAVDDVFQAKMMDMLKQTGRDQMVVGWYHSHPGFGCWLSSVDV
NTQKSFEQLNSRAVAVVVDPIQSVKGKVVIDAFRLIQALIHGLNRHYYSL
NIDYHKTAKETKMLMNLHKEQWQSGLKMYDYEEKEESNLAATKSMVKIAE
QYSKRIEEEKELTEEELKTRYVGRQDPKKHLSETADETLENNIVSVLTAG
VNSVAIK
3D structure
PDB3jck Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition.
ChainG
Resolution3.5 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 G H109 H111 D122 H86 H88 D99
Gene Ontology
Molecular Function
GO:0004843 cysteine-type deubiquitinase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008234 cysteine-type peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
GO:0046872 metal ion binding
GO:0070628 proteasome binding
GO:0140492 metal-dependent deubiquitinase activity
Biological Process
GO:0000266 mitochondrial fission
GO:0006508 proteolysis
GO:0016559 peroxisome fission
GO:0016579 protein deubiquitination
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0043248 proteasome assembly
GO:1902906 proteasome storage granule assembly
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005739 mitochondrion
GO:0005829 cytosol
GO:0008541 proteasome regulatory particle, lid subcomplex
GO:0034515 proteasome storage granule

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Molecular Function
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Cellular Component
External links
PDB RCSB:3jck, PDBe:3jck, PDBj:3jck
PDBsum3jck
PubMed26744777
UniProtP43588|RPN11_YEAST Ubiquitin carboxyl-terminal hydrolase RPN11 (Gene Name=RPN11)

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