X-ray diffraction
1.8Å resolution

Crystal structure of a diaminohydroxyphosphoribosylaminopyrimidine deaminase/ 5-amino-6-(5-phosphoribosylamino)uracil reductase (tm1828) from thermotoga maritima at 1.80 A resolution

Source organism: Thermotoga maritima
Entry author: Joint Center for Structural Genomics (JCSG)

Function and Biology Details

Reactions catalysed:
2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)pyrimidine + H(2)O = 5-amino-6-(5-phosphoribosylamino)uracil + NH(3)
5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH
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 RibD Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 40.67 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
  • Canonical: Q9X2E8 (Residues: 1-348; Coverage: 100%)
Gene name: TM_1828
Sequence domains:
Structure domains:

Ligands and Environments

Cofactor: Ligand NDP 1 x NDP
3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I422
Unit cell:
a: 104.18Å b: 104.18Å c: 145.89Å
α: 90° β: 90° γ: 90°
R R work R free
0.162 0.16 0.195
Expression system: Escherichia coli