PDBe 5cpa

X-ray diffraction
1.54Å resolution

REFINED CRYSTAL STRUCTURE OF CARBOXYPEPTIDASE A AT 1.54 ANGSTROMS RESOLUTION.

Released:
Source organism: Bos taurus
Primary publication:
Refined crystal structure of carboxypeptidase A at 1.54 A resolution.
J. Mol. Biol. 168 367-87 (1983)
PMID: 6887246

Function and Biology Details

Reaction catalysed:
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase A1 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 34.44 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P00730 (Residues: 111-417; Coverage: 76%)
Gene names: CPA, CPA1
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 51.6Å b: 60.27Å c: 47.25Å
α: 90° β: 97.27° γ: 90°
Expression system: Not provided