› 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:
DOI: 10.2210/pdb1pca/pdb
PDB entry 1pca coloured by chain, front view.
PDB entry 1pca coloured by chain, side view.
PDB entry 1pca coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.
Guasch A, Coll M, Avilés FX, Huber R
J Mol Biol 224 141-57 (1992)
PMID: 1548696

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
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140835 (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:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand CIT 1 x CIT
Ligand VAL 1 x VAL
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°

Quick links

Citations

7 review citations

Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes.
Khan et al. (1998)
6 more

19 mentions without citation

FOLD-RATE: prediction of protein folding rates from amino acid sequence.
Gromiha et al. (2006)
18 more