› 4qu3

X-ray diffraction
1.4Å resolution

GES-2 ertapenem acyl-enzyme complex

Released:
DOI: 10.2210/pdb4qu3/pdb
PDB entry 4qu3 coloured by chain, front view.
PDB entry 4qu3 coloured by chain, side view.
PDB entry 4qu3 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Kinetic and structural requirements for carbapenemase activity in GES-type β-lactamases.
Stewart NK, Smith CA, Frase H, Black DJ, Vakulenko SB
OpenAccess logo Biochemistry 54 588-97 (2015)
PMID: 25485972

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-188053 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase GES-2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 31.25 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93F76 (Residues: 1-287; Coverage: 100%)
Gene names: bla, blaGES-2
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

4 bound ligands:
Ligand 1RG 2 x 1RG
Ligand CA 1 x CA
Ligand IOD 6 x IOD
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 43.001Å b: 81.329Å c: 71.895Å
α: 90° β: 101.97° γ: 90°
R-values:
R R work R free
0.16 0.158 0.197
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The Collateral Effects of COVID-19 Pandemic on the Status of Carbapenemase-Producing Pathogens.
Ayoub Moubareck et al. (2022)
1 more

3 mentions without citation

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