› 1dor

X-ray diffraction
2Å resolution

DIHYDROOROTATE DEHYDROGENASE A FROM LACTOCOCCUS LACTIS

Released:
DOI: 10.2210/pdb1dor/pdb
PDB entry 1dor coloured by chain, front view.
PDB entry 1dor coloured by chain, side view.
PDB entry 1dor coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
The crystal structure of the flavin containing enzyme dihydroorotate dehydrogenase A from Lactococcus lactis.
Rowland P, Nielsen FS, Jensen KF, Larsen S
Structure 5 239-52 (1997)
PMID: 9032071

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106948 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Dihydroorotate dehydrogenase A (fumarate) Chains: A, B
Molecule details ›
Chains: A, B
Length: 311 amino acids
Theoretical weight: 34.24 KDa
Source organism: Lactococcus lactis
UniProt:
  • Canonical: A2RJT9 (Residues: 1-311; Coverage: 100%)
Gene names: llmg_0952, pyrDA
Sequence domains: Dihydroorotate dehydrogenase
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P21
Unit cell:
a: 54.19Å b: 109.23Å c: 67.17Å
α: 90° β: 104.5° γ: 90°
R-values:
R R work R free
0.168 0.168 0.212

Quick links

Citations

4 review citations

Nucleotide metabolism and its control in lactic acid bacteria.
Kilstrup et al. (2005)
3 more

6 mentions without citation

On the Natural History of Flavin-Based Electron Bifurcation.
Baymann et al. (2018)
5 more