› 1ysc

X-ray diffraction
2.8Å resolution

2.8 ANGSTROMS STRUCTURE OF YEAST SERINE CARBOXYPEPTIDASE

Released:
DOI: 10.2210/pdb1ysc/pdb
PDB entry 1ysc coloured by chain, front view.
PDB entry 1ysc coloured by chain, side view.
PDB entry 1ysc coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
2.8-A structure of yeast serine carboxypeptidase.
Endrizzi JA, Breddam K, Remington SJ
Biochemistry 33 11106-20 (1994)
PMID: 7727362

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: 47.36 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
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: 111.8Å b: 111.8Å c: 111.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 not available not available
Expression system: Not provided

Quick links

Citations

4 review citations

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
Khan et al. (1998)
3 more

7 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
6 more