› 2cig

X-ray diffraction
1.9Å resolution

Dihydrofolate reductase from Mycobacterium tuberculosis inhibited by the acyclic 4R isomer of INH-NADP a derivative of the prodrug isoniazid.

Released:
DOI: 10.2210/pdb2cig/pdb
PDB entry 2cig coloured by chain, front view.
PDB entry 2cig coloured by chain, side view.
PDB entry 2cig coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid.
Argyrou A, Vetting MW, Aladegbami B, Blanchard JS
Nat Struct Mol Biol 13 408-13 (2006)
PMID: 16648861

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161901 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 17.66 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WNX1 (Residues: 3-161; Coverage: 99%)
Gene names: MTV002.28c, Rv2763c, dfrA, folA
Sequence domains: Dihydrofolate reductase
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand 1DG 1 x 1DG
2 bound ligands:
Ligand GOL 4 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200B
Spacegroup: P41
Unit cell:
a: 60.67Å b: 60.67Å c: 59.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.212
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Antimicrobial susceptibility testing, drug resistance mechanisms, and therapy of infections with nontuberculous mycobacteria.
Brown-Elliott et al. (2012)
14 more

5 mentions without citation

PocketMatch: a new algorithm to compare binding sites in protein structures.
Yeturu et al. (2008)
4 more