› 1cg2

X-ray diffraction
2.5Å resolution

CARBOXYPEPTIDASE G2

Released:
DOI: 10.2210/pdb1cg2/pdb
PDB entry 1cg2 coloured by chain, front view.
PDB entry 1cg2 coloured by chain, side view.
PDB entry 1cg2 coloured by chain, top view.
Source organism: Pseudomonas sp. RS-16
Primary publication:
Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy.
Rowsell S, Pauptit RA, Tucker AD, Melton RG, Blow DM, Brick P
Structure 5 337-47 (1997)
PMID: 9083113

Function and Biology Details

Reaction catalysed: 
Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxypeptidase G2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 393 amino acids
Theoretical weight: 41.75 KDa
Source organism: Pseudomonas sp. RS-16
Expression system: Escherichia coli
UniProt:
  • Canonical: P06621 (Residues: 23-415; Coverage: 100%)
Gene name: cpg2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 13 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P21
Unit cell:
a: 81.26Å b: 105.28Å c: 122.19Å
α: 90° β: 109.54° γ: 90°
R-values:
R R work R free
0.196 0.196 0.224
Expression system: Escherichia coli

Quick links

Citations

11 review citations

How far divergent evolution goes in proteins.
Murzin AG. (1998)
10 more

16 mentions without citation

Crystal structure of prostate-specific membrane antigen, a tumor marker and peptidase.
Davis et al. (2005)
15 more