› 4gog

X-ray diffraction
1.1Å resolution

Crystal structure of the GES-1 imipenem acyl-enzyme complex

Released:
DOI: 10.2210/pdb4gog/pdb
PDB entry 4gog coloured by chain, front view.
PDB entry 4gog coloured by chain, side view.
PDB entry 4gog coloured by chain, top view.
Source organism: Klebsiella pneumoniae
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-191911 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase GES-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 31.19 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9KJY7 (Residues: 1-287; Coverage: 100%)
Gene names: blaGES-1, ges-1
Sequence domains:
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

3 bound ligands:
Ligand IM2 2 x IM2
Ligand IOD 19 x IOD
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P21
Unit cell:
a: 42.95Å b: 81.22Å c: 72.12Å
α: 90° β: 102.29° γ: 90°
R-values:
R R work R free
0.15 0.149 0.168
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural and Functional Aspects of Class A Carbapenemases.
Naas et al. (2016)
1 more

5 mentions without citation

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