› 4gnu

X-ray diffraction
1.09Å resolution

Crystal structure of GES-5 carbapenemase

Released:
DOI: 10.2210/pdb4gnu/pdb
PDB entry 4gnu coloured by chain, front view.
PDB entry 4gnu coloured by chain, side view.
PDB entry 4gnu coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural basis for progression toward the carbapenemase activity in the GES family of β-lactamases.
Smith CA, Frase H, Toth M, Kumarasiri M, Wiafe K, Munoz J, Mobashery S, Vakulenko SB
J Am Chem Soc 134 19512-5 (2012)
PMID: 23148776

Function and Biology Details

Reaction catalysed: 
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106068 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 31.22 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: A0EL75 (Residues: 1-287; Coverage: 100%)
Gene name: blaGES-5
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 42.66Å b: 80.47Å c: 71.23Å
α: 90° β: 101.48° γ: 90°
R-values:
R R work R free
0.157 0.156 0.172
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-Lactam antibiotic targets and resistance mechanisms: from covalent inhibitors to substrates.
Mora-Ochomogo et al. (2021)
1 more

7 mentions without citation

Structural basis for carbapenem-hydrolyzing mechanisms of carbapenemases conferring antibiotic resistance.
Jeon et al. (2015)
6 more