X-ray diffraction
2.3Å resolution

Crystal structure of bovine pancreatic carboxypeptidase A complexed with D-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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Carboxypeptidase A1 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 34.52 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: P21
Unit cell:
a: 51.961Å b: 60.465Å c: 47.792Å
α: 90° β: 97.59° γ: 90°
R R work R free
0.139 0.139 0.174