› 3fai

X-ray diffraction
1.7Å resolution

The Di Zinc Carbapenemase CphA N220G mutant

Released:
DOI: 10.2210/pdb3fai/pdb
PDB entry 3fai coloured by chain, front view.
PDB entry 3fai coloured by chain, side view.
PDB entry 3fai coloured by chain, top view.
Source organism: Aeromonas hydrophila
Primary publication:
The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.
Bebrone C, Delbrück H, Kupper MB, Schlömer P, Willmann C, Frère JM, Fischer R, Galleni M, Hoffmann KM
Antimicrob Agents Chemother 53 4464-71 (2009)
PMID: 19651913

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-150877 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Metallo-beta-lactamase type 2 Chain: A
Molecule details ›
Chain: A
Length: 227 amino acids
Theoretical weight: 25.16 KDa
Source organism: Aeromonas hydrophila
Expression system: Escherichia coli
UniProt:
  • Canonical: P26918 (Residues: 28-254; Coverage: 100%)
Gene name: cphA
Sequence domains: Metallo-beta-lactamase superfamily
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments

4 bound ligands:
Ligand ZN 3 x ZN
Ligand CL 7 x CL
Ligand SO4 7 x SO4
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR591
Spacegroup: C2221
Unit cell:
a: 42.68Å b: 101.06Å c: 116.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.14 0.139 0.16
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Carbapenems: past, present, and future.
Papp-Wallace et al. (2011)
9 more

2 mentions without citation

The structure of the dizinc subclass B2 metallo-beta-lactamase CphA reveals that the second inhibitory zinc ion binds in the histidine site.
Bebrone et al. (2009)
1 more