› 4gsq

X-ray diffraction
1.8Å resolution

Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains

Released:
DOI: 10.2210/pdb4gsq/pdb
PDB entry 4gsq coloured by chain, front view.
PDB entry 4gsq coloured by chain, side view.
PDB entry 4gsq coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural basis for the inhibition of Mycobacterium tuberculosis L,D-transpeptidase by meropenem, a drug effective against extensively drug-resistant strains.
Kim HS, Kim J, Im HN, Yoon JY, An DR, Yoon HJ, Kim JY, Min HK, Kim SJ, Lee JY, Han BW, Suh SW
Acta Crystallogr D Biol Crystallogr 69 420-31 (2013)
PMID: 23519417

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129428 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L,D-transpeptidase 2 Chain: A
Molecule details ›
Chain: A
Length: 287 amino acids
Theoretical weight: 31.28 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O53223 (Residues: 131-408; Coverage: 74%)
Gene names: MT2594, V735_02606, ldtB
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: C2
Unit cell:
a: 135.594Å b: 58.639Å c: 40.925Å
α: 90° β: 94.4° γ: 90°
R-values:
R R work R free
0.197 0.195 0.233
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The Mycobacterial Cell Wall--Peptidoglycan and Arabinogalactan.
Alderwick et al. (2015)
5 more

4 mentions without citation

Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.
Vermassen et al. (2019)
3 more