› 1fcm

X-ray diffraction
2.46Å resolution

CRYSTAL STRUCTURE OF THE E.COLI AMPC BETA-LACTAMASE MUTANT Q120L/Y150E COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, CLOXACILLIN

Released:
DOI: 10.2210/pdb1fcm/pdb
PDB entry 1fcm coloured by chain, front view.
PDB entry 1fcm coloured by chain, side view.
PDB entry 1fcm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal Structures of Substrate and Inhibitor Complexes with AmpC -Lactamase: Possible Implications for Substrate-Assisted Catalysis
Patera A, Blaszczak LC, Shoichet BK
J. Am. Chem. Soc. 122 10504-10512 (2000)

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: 39.54 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 CXU 2 x CXU
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 118.52Å b: 76.19Å c: 98.28Å
α: 90° β: 116.68° γ: 90°
R-values:
R R work R free
0.207 0.207 0.265
Expression system: Escherichia coli

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Citations

2 mentions without citation

Conformational Change Observed in the Active Site of Class C β-Lactamase MOX-1 upon Binding to Aztreonam.
Oguri et al. (2015)
1 more