› 1cpy

X-ray diffraction
2.6Å resolution

SITE-DIRECTED MUTAGENESIS ON (SERINE) CARBOXYPEPTIDASE Y FROM YEAST. THE SIGNIFICANCE OF THR 60 AND MET 398 IN HYDROLYSIS AND AMINOLYSIS REACTIONS

Released:
DOI: 10.2210/pdb1cpy/pdb
PDB entry 1cpy coloured by chain, front view.
PDB entry 1cpy coloured by chain, side view.
PDB entry 1cpy coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Site-Directed Mutagenesis on (Serine) Carboxypeptidase Y from Yeast. The Significance of Thr 60 and met 398 in Hydrolysis and Aminolysis Reactions
Sorensen SB, Raaschou-Nielsen M, Mortensen UH, Remington SJ, Breddam K
J. Am. Chem. Soc. 117 5944-5950 (1995)

Function and Biology Details

Reaction catalysed: 
Release of a C-terminal amino acid with broad specificity.
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-133043 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase Y Chain: A
Molecule details ›
Chain: A
Length: 421 amino acids
Theoretical weight: 47.24 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P00729 (Residues: 112-532; Coverage: 82%)
Gene names: PRC1, YMR297W
Sequence domains: Serine carboxypeptidase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NAG 3 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P213
Unit cell:
a: 112Å b: 112Å c: 112Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 not available not available

Quick links

Citations

3 mentions without citation

Large-scale protein structure modeling of the Saccharomyces cerevisiae genome.
Sánchez et al. (1998)
2 more