› 2lx5

Solution NMR

NMR solution structure of peptide epsilon(103-120) from Mycobacterium tuberculosis F-ATPsynthase

Released:
DOI: 10.2210/pdb2lx5/pdb
PDB entry 2lx5 coloured by chain, ensemble of 20 models, front view.
PDB entry 2lx5 coloured by chain, ensemble of 20 models, side view.
PDB entry 2lx5 coloured by chain, ensemble of 20 models, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Variations of subunit {varepsilon} of the Mycobacterium tuberculosis F1Fo ATP synthase and a novel model for mechanism of action of the tuberculosis drug TMC207.
Biukovic G, Basak S, Manimekalai MS, Rishikesan S, Roessle M, Dick T, Rao SP, Hunke C, Grüber G
Antimicrob Agents Chemother 57 168-76 (2013)
PMID: 23089752

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162009 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP synthase epsilon chain Chain: A
Molecule details ›
Chain: A
Length: 18 amino acids
Theoretical weight: 1.92 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Not provided
UniProt:
  • Canonical: P9WPV1 (Residues: 103-120; Coverage: 15%)
Gene names: MTCY373.31, Rv1311, atpC

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this NMR entry.
Chemical shift assignment: 42%
Refinement method: simulated annealing
Expression system: Not provided

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Citations

14 review citations

Advances in the development of new tuberculosis drugs and treatment regimens.
Zumla et al. (2013)
13 more

2 mentions without citation

Solution NMR Studies of Mycobacterium tuberculosis Proteins for Antibiotic Target Discovery.
Kim et al. (2017)
1 more