› 3i68

X-ray diffraction
2.4Å resolution

Plasmodium falciparum dihydroorotate dehydrogenase bound with triazolopyrimidine-based inhibitor DSM2

Released:
DOI: 10.2210/pdb3i68/pdb
PDB entry 3i68 coloured by chain, front view.
PDB entry 3i68 coloured by chain, side view.
PDB entry 3i68 coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Structural plasticity of malaria dihydroorotate dehydrogenase allows selective binding of diverse chemical scaffolds.
Deng X, Gujjar R, El Mazouni F, Kaminsky W, Malmquist NA, Goldsmith EJ, Rathod PK, Phillips MA
J Biol Chem 284 26999-7009 (2009)
PMID: 19640844

Function and Biology Details

Reaction catalysed: 
(S)-dihydroorotate + a quinone = orotate + a quinol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170607 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase (quinone), mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 415 amino acids
Theoretical weight: 46.65 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08210 (Residues: 158-569; Coverage: 67%)
Gene name: PFF0160c
Sequence domains: Dihydroorotate dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
2 bound ligands:
Ligand J4Z 1 x J4Z
Ligand ORO 1 x ORO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P64
Unit cell:
a: 85.917Å b: 85.917Å c: 138.697Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.224 0.214 0.267
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Malaria medicines: a glass half full?
Wells et al. (2015)
7 more

6 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
5 more