› 4kl9

X-ray diffraction
1.39Å resolution

Crystal structure of dihydrofolate reductase from Mycobacterium tuberculosis in the space group C2

Released:
DOI: 10.2210/pdb4kl9/pdb
PDB entry 4kl9 coloured by chain, front view.
PDB entry 4kl9 coloured by chain, side view.
PDB entry 4kl9 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Mycobacterium tuberculosis dihydrofolate reductase reveals two conformational states and a possible low affinity mechanism to antifolate drugs.
Dias MV, Tyrakis P, Domingues RR, Paes Leme AF, Blundell TL
Structure 22 94-103 (2014)
PMID: 24210757

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydrofolate reductase Chain: A
Molecule details ›
Chain: A
Length: 179 amino acids
Theoretical weight: 19.83 KDa
Source organism: Mycobacterium tuberculosis
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 NDP 1 x NDP
1 bound ligand:
Ligand P33 1 x P33
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 67.58Å b: 73.59Å c: 36.83Å
α: 90° β: 98.77° γ: 90°
R-values:
R R work R free
0.157 0.155 0.202
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Mycobacterium tuberculosis folate metabolism and the mechanistic basis for para-aminosalicylic acid susceptibility and resistance.
Minato et al. (2015)
2 more

3 mentions without citation

Predicting Displaceable Water Sites Using Mixed-Solvent Molecular Dynamics.
Graham et al. (2018)
2 more