1t6y

X-ray diffraction
2.8Å resolution

Crystal structure of ADP, AMP, and FMN bound TM379

Released:
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
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 BL21(DE3)
UniProt:
  • Canonical: Q9WZW1 (Residues: 1-293; Coverage: 100%)
Gene name: TM_0857
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FMN 2 x FMN
2 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: 67.803Å b: 82.661Å c: 66.717Å
α: 90° β: 116.42° γ: 90°
R-values:
R R work R free
0.238 0.231 0.298
Expression system: Escherichia coli BL21(DE3)