› 1f76

X-ray diffraction
2.5Å resolution

ESCHERICHIA COLI DIHYDROOROTATE DEHYDROGENASE

Released:
DOI: 10.2210/pdb1f76/pdb
PDB entry 1f76 coloured by chain, front view.
PDB entry 1f76 coloured by chain, side view.
PDB entry 1f76 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
E. coli dihydroorotate dehydrogenase reveals structural and functional distinctions between different classes of dihydroorotate dehydrogenases.
Nørager S, Jensen KF, Björnberg O, Larsen S
Structure 10 1211-23 (2002)
PMID: 12220493

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-141586 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase (quinone) Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 336 amino acids
Theoretical weight: 37.15 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7E1 (Residues: 1-336; Coverage: 100%)
Gene names: JW0928, b0945, pyrD
Sequence domains: Dihydroorotate dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 4 x FMN
2 bound ligands:
Ligand ORO 3 x ORO
Ligand FMT 8 x FMT
1 modified residue:
Ligand MSE 28 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM30A
Spacegroup: P41212
Unit cell:
a: 119.7Å b: 119.7Å c: 295.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.217
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Plasmodium dihydroorotate dehydrogenase: a promising target for novel anti-malarial chemotherapy.
Phillips et al. (2010)
3 more

15 mentions without citation

The two sides of a lipid-protein story.
Basso et al. (2016)
14 more