› 1rgy

X-ray diffraction
1.52Å resolution

Citrobacter freundii GN346 Class C beta-Lactamase Complexed with Transition-State Analog of Cefotaxime

Released:
DOI: 10.2210/pdb1rgy/pdb
PDB entry 1rgy coloured by chain, front view.
PDB entry 1rgy coloured by chain, side view.
PDB entry 1rgy coloured by chain, top view.
Source organism: Citrobacter freundii
Primary publication:
Hydrolysis of third-generation cephalosporins by class C beta-lactamases. Structures of a transition state analog of cefotoxamine in wild-type and extended spectrum enzymes.
Nukaga M, Kumar S, Nukaga K, Pratt RF, Knox JR
J Biol Chem 279 9344-52 (2004)
PMID: 14660590

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-138582 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 39.83 KDa
Source organism: Citrobacter freundii
Expression system: Escherichia coli
UniProt:
  • Canonical: P05193 (Residues: 22-381; Coverage: 100%)
Gene names: ampC, blaC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
Ligand PTX 1 x PTX
Ligand MPD 1 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL40B2
Spacegroup: P212121
Unit cell:
a: 59Å b: 72.23Å c: 86.81Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Three decades of beta-lactamase inhibitors.
Drawz et al. (2010)
3 more

5 mentions without citation

ClbP is a prototype of a peptidase subgroup involved in biosynthesis of nonribosomal peptides.
Dubois et al. (2011)
4 more