› 1yme

X-ray diffraction
1.53Å resolution

STRUCTURE OF CARBOXYPEPTIDASE

Released:
DOI: 10.2210/pdb1yme/pdb
PDB entry 1yme coloured by chain, front view.
PDB entry 1yme coloured by chain, side view.
PDB entry 1yme coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Carboxypeptidase A: native, zinc-removed and mercury-replaced forms.
Greenblatt HM, Feinberg H, Tucker PA, Shoham G
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
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: 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 ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 51.62Å b: 60.17Å c: 47.17Å
α: 90° β: 97.4° γ: 90°
R-values:
R R work R free
0.148 0.148 not available

Quick links

Citations

6 citation in other articles

Identifying cysteines and histidines in transition-metal-binding sites using support vector machines and neural networks.
Passerini et al. (2006)
5 more

8 mentions without citation

Peptide-plane flipping in proteins.
Hayward S. (2001)
7 more