5mut

X-ray diffraction
1.75Å resolution

Crystal structure of potent human Dihydroorotate Dehydrogenase inhibitors based on hydroxylated azole scaffolds

Released:
Source organism: Homo sapiens
Entry authors: Goyal P, Andersson M, Moritzer AC, Sainas S, Pippione AC, Boschi D, Al-Kadaraghi S, Lolli M, Friemann R

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase (quinone), mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 365 amino acids
Theoretical weight: 39.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q02127 (Residues: 31-395; Coverage: 92%)
Gene name: DHODH
Sequence domains: Dihydroorotate dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3221
Unit cell:
a: 91.08Å b: 91.08Å c: 122.522Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.17 0.168 0.198
Expression system: Escherichia coli BL21(DE3)