› 1vhn

X-ray diffraction
1.59Å resolution

Crystal structure of a putative flavin oxidoreductase with flavin

Released:
DOI: 10.2210/pdb1vhn/pdb
PDB entry 1vhn coloured by chain, front view.
PDB entry 1vhn coloured by chain, side view.
PDB entry 1vhn coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
The 1.59 A resolution crystal structure of TM0096, a flavin mononucleotide binding protein from Thermotoga maritima.
Park F, Gajiwala K, Noland B, Wu L, He D, Molinari J, Loomis K, Pagarigan B, Kearins P, Christopher J, Peat T, Badger J, Hendle J, Lin J, Buchanan S
Proteins 55 772-4 (2004)
PMID: 15103641

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194440 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA-dihydrouridine synthase Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 36.9 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WXV1 (Residues: 2-306; Coverage: 100%)
Gene name: TM_0096
Sequence domains: Dihydrouridine synthase (Dus)
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand FMN 1 x FMN
1 modified residue:
Ligand MSE 7 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: C2221
Unit cell:
a: 80.279Å b: 96.442Å c: 93.139Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.227
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
Conners et al. (2006)
1 more

5 mentions without citation

Molecular evolution of dihydrouridine synthases.
Kasprzak et al. (2012)
4 more