PDBe 1m4l

X-ray diffraction
1.25Å resolution

STRUCTURE OF NATIVE CARBOXYPEPTIDASE A AT 1.25 RESOLUTION

Released:
Source organism: Bos taurus
Primary publication:
Refined structure of bovine carboxypeptidase A at 1.25 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 59 323-33 (2003)
PMID: 12554943

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: 34.45 KDa
Source organism: Bos taurus
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
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P21
Unit cell:
a: 51.687Å b: 60.267Å c: 47.453Å
α: 90° β: 97.47° γ: 90°
R-values:
R R work R free
0.104 0.104 0.145