1arm

X-ray diffraction
1.76Å resolution

CARBOXYPEPTIDASE A WITH ZN REPLACED BY HG

Released:
Source organism: Bos taurus
Primary publication:
Carboxypeptidase A: native, zinc-removed and mercury-replaced forms.
Acta Crystallogr. D Biol. Crystallogr. 54 289-305 (1998)
PMID: 9867434

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: 309 amino acids
Theoretical weight: 34.72 KDa
Source organism: Bos taurus
UniProt:
  • Canonical: P00730 (Residues: 111-419; Coverage: 77%)
Gene names: CPA, CPA1
Sequence domains: Zinc carboxypeptidase
Structure domains: Zn peptidases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 51.7Å b: 60.32Å c: 47.2Å
α: 90° β: 97.39° γ: 90°