PDBe 5hvi

X-ray diffraction
1.64Å resolution

Crystal structure of TEM1 beta-lactamase

Released:
Source organism: Escherichia coli
Entry authors: Roose BW, Dmochowski IJ

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 TEM Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 263 amino acids
Theoretical weight: 28.91 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P62593 (Residues: 24-286; Coverage: 100%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6
Sequence domains: Beta-lactamase enzyme family

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P21
Unit cell:
a: 60.663Å b: 84.156Å c: 95.703Å
α: 90° β: 90.07° γ: 90°
R-values:
R R work R free
0.169 0.167 0.206
Expression system: Escherichia coli