› 1ac5

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF KEX1(DELTA)P, A PROHORMONE-PROCESSING CARBOXYPEPTIDASE FROM SACCHAROMYCES CEREVISIAE

Released:
DOI: 10.2210/pdb1ac5/pdb
PDB entry 1ac5 coloured by chain, front view.
PDB entry 1ac5 coloured by chain, side view.
PDB entry 1ac5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of Kex1deltap, a prohormone-processing carboxypeptidase from Saccharomyces cerevisiae,
Shilton BH, Thomas DY, Cygler M
Biochemistry 36 9002-12 (1997)
PMID: 9220988

Function and Biology Details

Reaction catalysed: 
Preferential release of a C-terminal arginine or lysine residue.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140716 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Pheromone-processing carboxypeptidase KEX1 Chain: A
Molecule details ›
Chain: A
Length: 483 amino acids
Theoretical weight: 54.27 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P09620 (Residues: 23-505; Coverage: 68%)
Gene names: KEX1, YGL203C
Sequence domains: Serine carboxypeptidase
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
1 bound ligand:
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 57.15Å b: 83.05Å c: 111.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.195 0.25

Quick links

Citations

1 review citation

The viral killer system in yeast: from molecular biology to application.
Schmitt et al. (2002)
6 other articles

8 mentions without citation

Identification, analysis, and prediction of protein ubiquitination sites.
Radivojac et al. (2010)
7 more