› 1l2s

X-ray diffraction
1.94Å resolution

X-ray crystal structure of AmpC beta-lactamase from E. coli in complex with a DOCK-predicted non-covalent inhibitor

Released:
DOI: 10.2210/pdb1l2s/pdb
PDB entry 1l2s coloured by chain, front view.
PDB entry 1l2s coloured by chain, side view.
PDB entry 1l2s coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure-based discovery of a novel, noncovalent inhibitor of AmpC beta-lactamase.
Powers RA, Morandi F, Shoichet BK
Structure 10 1013-23 (2002)
PMID: 12121656

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

1 bound ligand:
Ligand STC 3 x STC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 118.67Å b: 76.42Å c: 97.9Å
α: 90° β: 116.63° γ: 90°
R-values:
R R work R free
0.173 0.173 0.207
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Virtual screening of chemical libraries.
Shoichet BK. (2004)
13 more

26 mentions without citation

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