6fnu

X-ray diffraction
1.56Å resolution

Structure of S. cerevisiae Methylenetetrahydrofolate reductase 1, catalytic domain

Released:

Function and Biology Details

Reaction catalysed:
5-methyltetrahydrofolate + NAD(P)(+) = 5,10-methylenetetrahydrofolate + NAD(P)H
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Methylenetetrahydrofolate reductase 1 Chain: A
Molecule details ›
Chain: A
Length: 308 amino acids
Theoretical weight: 34.79 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P46151 (Residues: 1-302; Coverage: 46%)
Gene names: LPB8C, MET12, YPL023C
Sequence domains: Methylenetetrahydrofolate reductase
Structure domains: TIM Barrel

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21212
Unit cell:
a: 110.65Å b: 54.53Å c: 61.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.152 0.19
Expression system: Escherichia coli