› 8cpa

X-ray diffraction
2Å resolution

COMPARISON OF THE STRUCTURES OF THREE CARBOXYPEPTIDASE A-PHOSPHONATE COMPLEXES DETERMINED BY X-RAY CRYSTALLOGRAPHY

Released:
DOI: 10.2210/pdb8cpa/pdb
PDB entry 8cpa coloured by chain, front view.
PDB entry 8cpa coloured by chain, side view.
PDB entry 8cpa coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Comparison of the structures of three carboxypeptidase A-phosphonate complexes determined by X-ray crystallography.
Kim H, Lipscomb WN
Biochemistry 30 8171-80 (1991)
PMID: 1868092

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-133045 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase A1 Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 34.44 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • 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:
Ligand ZN 1 x ZN
Ligand AGF 1 x AGF
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 63.4Å b: 65.9Å c: 74.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.186 not available
Expression system: Not provided

Quick links

Citations

8 review citations

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

6 mentions without citation

Low barrier hydrogen bonds in protein structure and function.
Kemp et al. (2021)
5 more