› 7a6z

X-ray diffraction
1.3Å resolution

Structure of P226G BlaC from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb7a6z/pdb
Model geometry
Fit model/data
PDB entry 7a6z coloured by chain, front view.
PDB entry 7a6z coloured by chain, side view.
PDB entry 7a6z coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Conserved proline residues prevent dimerization and aggregation in the β-lactamase BlaC.
Chikunova A, Manley MP, Heijjer CN, Drenth CS, Cramer-Blok AJ, Ahmad MUD, Perrakis A, Ubbink M
OpenAccess logo Protein Sci 33 e4972 (2024)
PMID: 38533527

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: 266 amino acids
Theoretical weight: 28.29 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

3 bound ligands:
Ligand GOL 8 x GOL
Ligand EDO 1 x EDO
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P212121
Unit cell:
a: 53.52Å b: 54.231Å c: 79.052Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.117 0.116 0.137
Expression system: Escherichia coli BL21(DE3)

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