› 4otk

X-ray diffraction
1.6Å resolution

A structural characterization of the isoniazid Mycobacterium tuberculosis drug target, Rv2971, in its unliganded form

Released:
DOI: 10.2210/pdb4otk/pdb
PDB entry 4otk coloured by chain, front view.
PDB entry 4otk coloured by chain, side view.
PDB entry 4otk coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
A structural characterization of the isoniazid Mycobacterium tuberculosis drug target, Rv2971, in its unliganded form.
Shahine A, Prasetyoputri A, Rossjohn J, Beddoe T
Acta Crystallogr F Struct Biol Commun 70 572-7 (2014)
PMID: 24817712

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aldo-keto reductase Rv2971 Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 34.19 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: P9WQA5 (Residues: 2-282; Coverage: 100%)
Gene name: Rv2971
Sequence domains: Aldo/keto reductase family
Structure domains: NADP-dependent oxidoreductase domain

Ligands and Environments

2 bound ligands:
Ligand MLI 2 x MLI
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P3221
Unit cell:
a: 86.27Å b: 86.27Å c: 86.29Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.147 0.146 0.168
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Using a Label Free Quantitative Proteomics Approach to Identify Changes in Protein Abundance in Multidrug-Resistant Mycobacterium tuberculosis.
Phong et al. (2015)

2 mentions without citation

A structural characterization of the isoniazid Mycobacterium tuberculosis drug target, Rv2971, in its unliganded form.
Shahine et al. (2014)
1 more