› 1kvl

X-ray diffraction
1.53Å resolution

X-ray Crystal Structure of AmpC S64G Mutant beta-Lactamase in Complex with Substrate and Product Forms of Cephalothin

Released:
DOI: 10.2210/pdb1kvl/pdb
PDB entry 1kvl coloured by chain, front view.
PDB entry 1kvl coloured by chain, side view.
PDB entry 1kvl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural milestones in the reaction pathway of an amide hydrolase: substrate, acyl, and product complexes of cephalothin with AmpC beta-lactamase.
Beadle BM, Trehan I, Focia PJ, Shoichet BK
Structure 10 413-24 (2002)
PMID: 12005439

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-133599 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.56 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 20-377; Coverage: 100%)
Gene names: JW4111, ampA, ampC, b4150
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

4 bound ligands:
Ligand PO4 2 x PO4
Ligand KCP 1 x KCP
Ligand CLS 1 x CLS
Ligand THN 1 x THN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 118.619Å b: 77.153Å c: 98.066Å
α: 90° β: 115.9° γ: 90°
R-values:
R R work R free
0.195 0.195 0.22
Expression system: Escherichia coli

Quick links

Citations

7 review citations

β-Lactamases and β-Lactamase Inhibitors in the 21st Century.
Tooke et al. (2019)
6 more

11 mentions without citation

Crystal structure of KPC-2: insights into carbapenemase activity in class A beta-lactamases.
Ke et al. (2007)
10 more