Structure of PDB 4y6v Chain N

Receptor sequence

>4y6vN (length=196) Species: 559292 (Saccharomyces cerevisiae S288C)

TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL

3D structure

• PDB: 4y6v Systematic Analyses of Substrate Preferences of 20S Proteasomes Using Peptidic Epoxyketone Inhibitors.
• Chain: N
• Resolution: 2.8 Å

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 G47	T1 T20 T21 G47
BS02	peptide	N	T1 S168	T1 S168
BS03	MG	N	I163 S169	I163 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

External links

• PDB: RCSB:4y6v, PDBe:4y6v, PDBj:4y6v
• PDBsum: 4y6v
• PubMed: 26020686
• UniProt: P38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)