1pca

X-ray diffraction
2Å resolution

THREE DIMENSIONAL STRUCTURE OF PORCINE PANCREATIC PROCARBOXYPEPTIDASE A. A COMPARISON OF THE A AND B ZYMOGENS AND THEIR DETERMINANTS FOR INHIBITION AND ACTIVATION

Released:

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: 403 amino acids
Theoretical weight: 45.3 KDa
Source organism: Sus scrofa
UniProt:
  • Canonical: P09954 (Residues: 16-418; Coverage: 100%)
Gene names: CPA, CPA1
Sequence domains: Carboxypeptidase activation peptide
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 127.06Å b: 76.92Å c: 47.52Å
α: 90° β: 90° γ: 90°