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X-ray diffraction
1.7Å resolution

X-ray crystal structure of AmpC beta-Lactamase (AmpC(D)) from an Escherichia coli with a Tripeptide Deletion (Gly286 Ser287 Asp288) on the H10 Helix

Released:

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181150 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 39.43 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: Q76DI4 (Residues: 20-374; Coverage: 100%)
Gene name: ampC
Sequence domains: Beta-lactamase
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU, PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P1
Unit cell:
a: 47.065Å b: 47.381Å c: 81.461Å
α: 82.62° β: 80.91° γ: 65.4°
R-values:
R R work R free
0.165 0.163 0.206
Expression system: Escherichia coli