› 1iel

X-ray diffraction
2Å resolution

Crystal Structure of AmpC beta-lactamase from E. coli in Complex with Ceftazidime

Released:
DOI: 10.2210/pdb1iel/pdb
PDB entry 1iel coloured by chain, front view.
PDB entry 1iel coloured by chain, side view.
PDB entry 1iel coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of ceftazidime and its transition-state analogue in complex with AmpC beta-lactamase: implications for resistance mutations and inhibitor design.
Powers RA, Caselli E, Focia PJ, Prati F, Shoichet BK
Biochemistry 40 9207-14 (2001)
PMID: 11478888

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: 39.59 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

2 bound ligands:
Ligand PO4 1 x PO4
Ligand CAZ 2 x CAZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: C2
Unit cell:
a: 118.49Å b: 77.04Å c: 98.07Å
α: 90° β: 115.76° γ: 90°
R-values:
R R work R free
0.182 0.182 0.226
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

16 mentions without citation

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