X-ray diffraction
1.2Å resolution

Crystal structure of chimeric beta-lactamase cTEM-19m at 1.2 angstrom resolution


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
Beta-lactamase PSE-4; Beta-lactamase TEM Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 28.83 KDa
Source organisms: Expression system: Escherichia coli
  • Canonical: P16897 (Residues: 63-68, 145-185; Coverage: 17%)
  • Canonical: P62593 (Residues: 24-65, 72-147, 189-286; Coverage: 82%)
Gene names: bla, blaT-3, blaT-4, blaT-5, blaT-6, carB1, pse4
Sequence domains: Beta-lactamase enzyme family
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: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 36.69Å b: 58.79Å c: 109.83Å
α: 90° β: 90° γ: 90°
R R work R free
0.107 0.105 0.138
Expression system: Escherichia coli