4ha9

X-ray diffraction
2.35Å resolution

Structural insights into the reduction mechanism of Saccharomyces cerevisia Riboflavin Biosynthesis Reductase Rib7

Released:

Function and Biology Details

Reaction catalysed:
2,5-diamino-6-(5-phospho-D-ribitylamino)pyrimidin-4(3H)-one + NAD(P)(+) = 2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 249 amino acids
Theoretical weight: 27.56 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P33312 (Residues: 1-244; Coverage: 100%)
Gene names: RIB7, YBR1203, YBR153W
Sequence domains: RibD C-terminal domain
Structure domains: Dihydrofolate Reductase, subunit A

Ligands and Environments


Cofactor: Ligand NDP 1 x NDP
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 45.978Å b: 68.868Å c: 150.335Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.265
Expression system: Escherichia coli