1li0

X-ray diffraction
1.61Å resolution

Crystal structure of TEM-32 beta-Lactamase at 1.6 Angstrom

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: null%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
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: APS BEAMLINE 5ID-B
Spacegroup: P212121
Unit cell:
a: 41.222Å b: 60.504Å c: 88.712Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.217
Expression system: Escherichia coli