Structure of PDB 3mg0 Chain N

Receptor sequence
>3mg0N (length=196) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
3D structure
PDB3mg0 Characterization of a new series of non-covalent proteasome inhibitors with exquisite potency and selectivity for the 20S beta5-subunit.
ChainN
Resolution2.68 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 BO2 N T1 T20 T21 T22 K33 R45 S46 G47 A49 T1 T20 T21 T22 K33 R45 S46 G47 A49
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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Biological Process
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Cellular Component
External links
PDB RCSB:3mg0, PDBe:3mg0, PDBj:3mg0
PDBsum3mg0
PubMed20632995
UniProtP38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)

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