› 6ddp

X-ray diffraction
1.49Å resolution

Mycobacterium tuberculosis Dihydrofolate Reductase complexed with beta-NADPH and 3'-[(2R)-4-(2,4-diamino-6-ethylpyrimidin-5-yl)but-3-yn-2-yl]-5'-methoxy[1,1'-biphenyl]-4-carboxylic acid

Released:
DOI: 10.2210/pdb6ddp/pdb
PDB entry 6ddp coloured by chain, front view.
PDB entry 6ddp coloured by chain, side view.
PDB entry 6ddp coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Drugging the Folate Pathway in Mycobacterium tuberculosis: The Role of Multi-targeting Agents.
Hajian B, Scocchera E, Shoen C, Krucinska J, Viswanathan K, G-Dayanandan N, Erlandsen H, Estrada A, Mikušová K, Korduláková J, Cynamon M, Wright D
Cell Chem Biol 26 781-791.e6 (2019)
PMID: 30930162

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 159 amino acids
Theoretical weight: 17.66 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
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 4 x NDP
1 bound ligand:
Ligand G6Y 4 x G6Y
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: P1
Unit cell:
a: 57.77Å b: 60.552Å c: 60.637Å
α: 90.04° β: 90.02° γ: 90.03°
R-values:
R R work R free
0.203 0.203 0.225
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Multitargeting Compounds: A Promising Strategy to Overcome Multi-Drug Resistant Tuberculosis.
Stelitano et al. (2020)
2 more

3 mentions without citation

An Outline of the Latest Crystallographic Studies on Inhibitor-Enzyme Complexes for the Design and Development of New Therapeutics against Tuberculosis.
Mori et al. (2021)
2 more