6nvu

X-ray diffraction
2.5Å resolution

Crystal structure of TLA-1 extended spectrum Beta-lactamase in complex with Clavulanic Acid

Released:
Source organism: Escherichia coli
Entry authors: Rudino-Pinera E, Cifuentes-Castro VH, Rodriguez-Almazan C

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 277 amino acids
Theoretical weight: 31.06 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9X6W1 (Residues: 36-312; Coverage: 99%)
Gene name: tla-1
Sequence domains: Beta-lactamase enzyme family

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P41212
Unit cell:
a: 98.64Å b: 98.64Å c: 100.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.266
Expression system: Escherichia coli BL21(DE3)