› 7a5u

X-ray diffraction
1.5Å resolution

Structure of E37A BlaC from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb7a5u/pdb
PDB entry 7a5u coloured by chain, front view.
PDB entry 7a5u coloured by chain, side view.
PDB entry 7a5u coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Conserved residues Glu37 and Trp229 play an essential role in protein folding of β-lactamase.
Chikunova A, Manley MP, Ud Din Ahmad M, Bilman T, Perrakis A, Ubbink M
FEBS J 288 5708-5722 (2021)
PMID: 33792206

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161732 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-lactamase Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 29.47 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WKD3 (Residues: 43-307; Coverage: 97%)
Gene names: MTCY49.07c, Rv2068c, blaA, blaC
Sequence domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand OCS 1 x OCS

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE MASSIF-1
Spacegroup: P21
Unit cell:
a: 38.56Å b: 54.739Å c: 54.509Å
α: 90° β: 95° γ: 90°
R-values:
R R work R free
0.127 0.125 0.176
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The biogenesis of β-lactamase enzymes.
Kaderabkova et al. (2022)
3 other articles

1 mention without citation

Conserved residues Glu37 and Trp229 play an essential role in protein folding of β-lactamase.
Chikunova et al. (2021)