› 1gce

X-ray diffraction
1.8Å resolution

STRUCTURE OF THE BETA-LACTAMASE OF ENTEROBACTER CLOACAE GC1

Released:
DOI: 10.2210/pdb1gce/pdb
PDB entry 1gce coloured by chain, front view.
PDB entry 1gce coloured by chain, side view.
PDB entry 1gce coloured by chain, top view.
Source organism: Enterobacter cloacae
Primary publication:
Structure of the extended-spectrum class C beta-lactamase of Enterobacter cloacae GC1, a natural mutant with a tandem tripeptide insertion.
Crichlow GV, Kuzin AP, Nukaga M, Mayama K, Sawai T, Knox JR
Biochemistry 38 10256-61 (1999)
PMID: 10441119

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-138639 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 364 amino acids
Theoretical weight: 39.61 KDa
Source organism: Enterobacter cloacae
Expression system: Escherichia coli
UniProt:
  • Canonical: P05364 (Residues: 21-230, 231-381; Coverage: 100%)
Gene name: ampC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21212
Unit cell:
a: 77.975Å b: 69.514Å c: 63.142Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.202 0.232
Expression system: Escherichia coli

Quick links

Citations

9 review citations

AmpC beta-lactamases.
Jacoby GA. (2009)
8 more

7 mentions without citation

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