› 1s4m

X-ray diffraction
2.1Å resolution

Crystal structure of flavin binding to FAD synthetase from Thermotoga maritina

Released:
DOI: 10.2210/pdb1s4m/pdb
PDB entry 1s4m coloured by chain, front view.
PDB entry 1s4m coloured by chain, side view.
PDB entry 1s4m coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structure of flavin binding to FAD synthetase of Thermotoga maritima.
Wang W, Kim R, Yokota H, Kim SH
Proteins 58 246-8 (2005)
PMID: 15468322

Function and Biology Details

Reactions catalysed: 
ATP + riboflavin = ADP + FMN
ATP + FMN = diphosphate + FAD
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194648 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Riboflavin biosynthesis protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 293 amino acids
Theoretical weight: 33.67 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZW1 (Residues: 1-293; Coverage: 100%)
Gene name: TM_0857
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand LUM 2 x LUM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 66.093Å b: 82.163Å c: 66.754Å
α: 90° β: 116.57° γ: 90°
R-values:
R R work R free
0.223 0.212 0.259
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Genetic control of biosynthesis and transport of riboflavin and flavin nucleotides and construction of robust biotechnological producers.
Abbas et al. (2011)
5 more

5 mentions without citation

The Recognition of Identical Ligands by Unrelated Proteins.
Barelier et al. (2015)
4 more