3upo

X-ray diffraction
2.3Å resolution

Structure of penicillin-binding protein A from M. tuberculosis: penicillin G acyl-enzyme complex

Released:

Function and Biology Details

Reaction catalysed:
Preferential cleavage: (Ac)(2)-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-161731 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidoglycan D,D-transpeptidase PbpA Chains: A, B
Molecule details ›
Chains: A, B
Length: 462 amino acids
Theoretical weight: 48.46 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WKD1 (Residues: 35-491; Coverage: 93%)
Gene names: MTCY10H4.16c, Rv0016c, pbpA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P61
Unit cell:
a: 123.21Å b: 123.21Å c: 97.32Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.195 0.243
Expression system: Escherichia coli BL21(DE3)