3lo7

X-ray diffraction
2.05Å resolution

Crystal structure of PBPA from Mycobacterium tuberculosis

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: 483 amino acids
Theoretical weight: 51.15 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WKD1 (Residues: 35-491; Coverage: 93%)
Gene names: MTCY10H4.16c, Rv0016c, pbpA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P61
Unit cell:
a: 120.6Å b: 120.6Å c: 92.2Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.215 0.252
Expression system: Escherichia coli