PDBe 5hw5

X-ray diffraction
1.41Å resolution

Crystal structure of TEM1 beta-lactamase in the presence of 2.0 MPa xenon

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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P21
Unit cell:
a: 60.44Å b: 84.62Å c: 96.011Å
α: 90° β: 90.58° γ: 90°
R-values:
R R work R free
0.186 0.184 0.221
Expression system: Escherichia coli