Structure of PDB 4nnw Chain N

Receptor sequence
>4nnwN (length=196) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL
3D structure
PDB4nnw Systematic Comparison of Peptidic Proteasome Inhibitors Highlights the alpha-Ketoamide Electrophile as an Auspicious Reversible Lead Motif.
ChainN
Resolution2.6 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 2MK N T1 T20 T21 T22 K33 G47 A49 T1 T20 T21 T22 K33 G47 A49
BS02 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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Biological Process
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Cellular Component
External links
PDB RCSB:4nnw, PDBe:4nnw, PDBj:4nnw
PDBsum4nnw
PubMed24403024
UniProtP38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)

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