X-ray diffraction
1.75Å resolution

Crystal structure of bovine pancreatic carboxypeptidase A complexed with L-N-hydroxyaminocarbonyl phenylalanine at 2.3 A


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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Carboxypeptidase A1 Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 307 amino acids
Theoretical weight: 34.44 KDa
Source organism: Bos taurus
  • Canonical: P00730 (Residues: 111-417; Coverage: 76%)
Gene names: CPA, CPA1
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 65.57Å b: 60.524Å c: 74.41Å
α: 90° β: 97.84° γ: 90°
R R work R free
0.198 0.198 0.229