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X-ray diffraction
2Å resolution

CADMIUM-SUBSTITUTED BOVINE PACREATIC CARBOXYPEPTIDASE A (ALFA-FORM) AT PH 5.5 AND 2 MM CHLORIDE IN MONOCLINIC CRYSTAL FORM.

Released:
DOI: 10.2210/pdb1elm/pdb
PDB entry 1elm coloured by chain, front view.
PDB entry 1elm coloured by chain, side view.
PDB entry 1elm coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Three high-resolution crystal structures of cadmium-substituted carboxypeptidase A provide insight into the enzymatic function.
Jensen F, Bukrinsky T, Bjerrum J, Larsen S
J Biol Inorg Chem 7 490-9 (2002)
PMID: 11941507

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: P
Molecule details ›
Chain: P
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

1 bound ligand:
Ligand CD 2 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 47.163Å b: 60.244Å c: 51.746Å
α: 90° β: 97.41° γ: 90°
R-values:
R R work R free
0.161 0.161 0.186

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Citations

2 review citations

Progress in metallocarboxypeptidases and their small molecular weight inhibitors.
Fernández et al. (2010)
1 more