› 1uuo

X-ray diffraction
2.44Å resolution

Rat dihydroorotate dehydrogenase (DHOD)in complex with brequinar

Released:
DOI: 10.2210/pdb1uuo/pdb
PDB entry 1uuo coloured by chain, front view.
PDB entry 1uuo coloured by chain, side view.
PDB entry 1uuo coloured by chain, top view.
Source organism: Rattus rattus
Primary publication:
Inhibitor binding in a class 2 dihydroorotate dehydrogenase causes variations in the membrane-associated N-terminal domain.
Hansen M, Le Nours J, Johansson E, Antal T, Ullrich A, Löffler M, Larsen S
Protein Sci 13 1031-42 (2004)
PMID: 15044733

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179032 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase (quinone), mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 40.34 KDa
Source organism: Rattus rattus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q63707 (Residues: 30-395; Coverage: 93%)
Gene name: Dhodh
Sequence domains: Dihydroorotate dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
4 bound ligands:
Ligand BRF 1 x BRF
Ligand ORO 1 x ORO
Ligand NI 1 x NI
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I711
Spacegroup: C2221
Unit cell:
a: 49.753Å b: 95.801Å c: 144.469Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.21 0.263
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Dihydroorotate dehydrogenase: A drug target for the development of antimalarials.
Singh et al. (2017)
34 other articles

7 mentions without citation

Chemistry and biology of multicomponent reactions.
Dömling et al. (2012)
6 more