› 1x8h

X-ray diffraction
1.6Å resolution

The Mono-Zinc Carbapenemase CphA (N220G mutant) Shows a Zn(II)- NH2 ARG Coordination

Released:
DOI: 10.2210/pdb1x8h/pdb
PDB entry 1x8h coloured by chain, front view.
PDB entry 1x8h coloured by chain, side view.
PDB entry 1x8h coloured by chain, top view.
Source organism: Aeromonas hydrophila
Primary publication:
A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem.
Garau G, Bebrone C, Anne C, Galleni M, Frère JM, Dideberg O
J Mol Biol 345 785-95 (2005)
PMID: 15588826

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 228 amino acids
Theoretical weight: 25.25 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 1 x ZN
Ligand CO3 1 x CO3
Ligand SO4 3 x SO4
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: C2221
Unit cell:
a: 42.683Å b: 101.286Å c: 117.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.153 0.18
Expression system: Escherichia coli

Quick links

Citations

32 review citations

Metallo-beta-lactamases: the quiet before the storm?
Walsh et al. (2005)
31 more

3 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)
2 more