X-ray diffraction
2.4Å resolution

Crystal structure of riboflavin bound TM379

Source organism: Thermotoga maritima
Entry authors: Shin DH, Wang W, Kim R, Yokota H, Kim S-H, Berkeley Structural Genomics Center (BSGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
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 BL21(DE3)
  • Canonical: Q9WZW1 (Residues: 1-293; Coverage: 100%)
Gene name: TM_0857
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 66.535Å b: 81.943Å c: 66.709Å
α: 90° β: 116.96° γ: 90°
R R work R free
0.232 0.225 0.295
Expression system: Escherichia coli BL21(DE3)