› 1fsy

X-ray diffraction
1.75Å resolution

AMPC BETA-LACTAMASE FROM E. COLI COMPLEXED WITH INHIBITOR CLOXACILLINBORONIC ACID

Released:
DOI: 10.2210/pdb1fsy/pdb
PDB entry 1fsy coloured by chain, front view.
PDB entry 1fsy coloured by chain, side view.
PDB entry 1fsy coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
Caselli E, Powers RA, Blasczcak LC, Wu CY, Prati F, Shoichet BK
Chem Biol 8 17-31 (2001)
PMID: 11182316

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133600 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 358 amino acids
Theoretical weight: 39.53 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P00811 (Residues: 20-376; 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 105 2 x 105
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 5ID-B
Spacegroup: C2
Unit cell:
a: 118.36Å b: 77.57Å c: 97.46Å
α: 90° β: 116.18° γ: 90°
R-values:
R R work R free
0.196 0.196 0.218
Expression system: Escherichia coli

Quick links

Citations

8 review citations

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

1 mention without citation

Saturation mutagenesis of Asn152 reveals a substrate selectivity switch in P99 cephalosporinase.
Lefurgy et al. (2007)