› 1ep3

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF LACTOCOCCUS LACTIS DIHYDROOROTATE DEHYDROGENASE B. DATA COLLECTED UNDER CRYOGENIC CONDITIONS.

Released:
DOI: 10.2210/pdb1ep3/pdb
PDB entry 1ep3 coloured by chain, front view.
PDB entry 1ep3 coloured by chain, side view.
PDB entry 1ep3 coloured by chain, top view.
Source organism: Lactococcus lactis
Primary publication:
Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster.
Rowland P, Nørager S, Jensen KF, Larsen S
Structure 8 1227-38 (2000)
PMID: 11188687

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157010 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 311 amino acids
Theoretical weight: 32.98 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: P54322 (Residues: 1-311; Coverage: 100%)
Gene names: llmg_1106, pyrDB
Sequence domains: Dihydroorotate dehydrogenase
Structure domains: Aldolase class I
Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit Chain: B
Molecule details ›
Chain: B
Length: 262 amino acids
Theoretical weight: 28.69 KDa
Source organism: Lactococcus lactis
Expression system: Escherichia coli
UniProt:
  • Canonical: P56968 (Residues: 1-262; Coverage: 100%)
Gene names: llmg_1105, pyrK
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN

Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand FES 1 x FES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: R32
Unit cell:
a: 199.89Å b: 199.89Å c: 80.27Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.195 0.237
Expression system: Escherichia coli

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