3nbl

X-ray diffraction
2Å resolution

Crystal Structure of BlaC-E166A covalently bound with Cefuroxime

Released:
Source organism: Mycobacterium tuberculosis
Entry authors: Tremblay LW, Blanchard JS

Function and Biology Details

Reaction catalysed:
A beta-lactam + H(2)O = a substituted beta-amino acid
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 265 amino acids
Theoretical weight: 28.21 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WKD3 (Residues: 43-307; Coverage: 97%)
Gene names: MTCY49.07c, Rv2068c, blaA, blaC
Sequence domains: Beta-lactamase enzyme family
Structure domains: DD-peptidase/beta-lactamase superfamily

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C, NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 49.383Å b: 68.102Å c: 75.652Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.181 0.222
Expression system: Escherichia coli