Structure of PDB 3sdi Chain N

Receptor sequence

>3sdiN (length=196) Species: 559292 (Saccharomyces cerevisiae S288C)

TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAA
DTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVA
GYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEE
TVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL

3D structure

• PDB: 3sdi Optimization of a series of dipeptides with a P3 threonine residue as non-covalent inhibitors of the chymotrypsin-like activity of the human 20S proteasome.
• Chain: N
• Resolution: 2.65 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	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:3sdi, PDBe:3sdi, PDBj:3sdi
• PDBsum: 3sdi
• PubMed: 20875739
• UniProt: P38624|PSB1_YEAST Proteasome subunit beta type-1 (Gene Name=PRE3)