Structure of PDB 4y77 Chain N

Receptor sequence
>4y77N (length=196) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
3D structure
PDB4y77 Systematic Analyses of Substrate Preferences of 20S Proteasomes Using Peptidic Epoxyketone Inhibitors.
ChainN
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) T1 D17 R19 K33 G47 S129 D166 S169
Catalytic site (residue number reindexed from 1) T1 D17 R19 K33 G47 S129 D166 S169
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 peptide N T1 T20 T21 T22 T31 K33 R45 G47 A49 T1 T20 T21 T22 T31 K33 R45 G47 A49
BS02 peptide N T1 S168 T1 S168
BS03 MG N I163 D166 S169 I163 D166 S169
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004298 threonine-type endopeptidase activity
GO:0005515 protein binding
Biological Process
GO:0006508 proteolysis
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:0005829 cytosol
GO:0005839 proteasome core complex
GO:0019774 proteasome core complex, beta-subunit complex
GO:0034515 proteasome storage granule

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Molecular Function
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Cellular Component
External links
PDB RCSB:4y77, PDBe:4y77, PDBj:4y77
PDBsum4y77
PubMed26020686
UniProtP38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)

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