Structure of PDB 4r02 Chain J

Receptor sequence
>4r02J (length=195) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEA
GDTVQFAEYIQANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQV
NVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRP
DMTTEEGLDLLKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDF
3D structure
PDB4r02 alpha-Keto Phenylamides as P1'-Extended Proteasome Inhibitors.
ChainJ
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S18 A20 K34 G48 Y135
Catalytic site (residue number reindexed from 1) S18 A20 K34 G48 Y135
Enzyme Commision number 3.4.25.1: proteasome endopeptidase complex.
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 MG J Q118 T124 Q118 T124
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0061133 endopeptidase activator activity
Biological Process
GO:0010498 proteasomal protein catabolic process
GO:0010499 proteasomal ubiquitin-independent protein catabolic process
GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
GO:0051603 proteolysis involved in protein catabolic process
Cellular Component
GO:0000502 proteasome complex
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005789 endoplasmic reticulum membrane
GO:0005829 cytosol
GO:0005839 proteasome core complex
GO:0019774 proteasome core complex, beta-subunit complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4r02, PDBe:4r02, PDBj:4r02
PDBsum4r02
PubMed25087721
UniProtP22141|PSB4_YEAST Proteasome subunit beta type-4 (Gene Name=PRE1)

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