› 4ef8

X-ray diffraction
1.56Å resolution

Crystal structure of dihydroorotate dehydrogenase from Leishmania major in complex with Phenyl isothiocyanate

Released:
DOI: 10.2210/pdb4ef8/pdb
PDB entry 4ef8 coloured by chain, front view.
PDB entry 4ef8 coloured by chain, side view.
PDB entry 4ef8 coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Target sites for the design of anti-trypanosomatid drugs based on the structure of dihydroorotate dehydrogenase.
Pinheiro MP, Emery Fda S, Nonato MC
Curr Pharm Des 19 2615-27 (2013)
PMID: 23116399

Function and Biology Details

Reaction catalysed: 
(S)-dihydroorotate + fumarate = orotate + succinate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175705 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase (fumarate) Chains: A, B
Molecule details ›
Chains: A, B
Length: 354 amino acids
Theoretical weight: 38.16 KDa
Source organism: Leishmania major
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4QEW7 (Residues: 1-320; Coverage: 100%)
Gene names: DHODH, LMJF_16_0530
Sequence domains: Dihydroorotate dehydrogenase
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
3 bound ligands:
Ligand 0FI 2 x 0FI
Ligand SO4 2 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P61
Unit cell:
a: 144.19Å b: 144.19Å c: 69.87Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.176 0.194
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Plasmodium falciparum dihydroorotate dehydrogenase: a drug target against malaria.
Hoelz et al. (2018)
8 other articles

3 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)
2 more