› 6fnu

X-ray diffraction
1.56Å resolution

Structure of S. cerevisiae Methylenetetrahydrofolate reductase 1, catalytic domain

Released:
DOI: 10.2210/pdb6fnu/pdb
PDB entry 6fnu coloured by chain, front view.
PDB entry 6fnu coloured by chain, side view.
PDB entry 6fnu coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition.
Froese DS, Kopec J, Rembeza E, Bezerra GA, Oberholzer AE, Suormala T, Lutz S, Chalk R, Borkowska O, Baumgartner MR, Yue WW
Nat Commun 9 2261 (2018)
PMID: 29891918

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155443 (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

Quick links

Citations

6 review citations

A Review of Small-Molecule Inhibitors of One-Carbon Enzymes: SHMT2 and MTHFD2 in the Spotlight.
Cuthbertson et al. (2021)
5 more

2 mentions without citation

Structural basis for the regulation of human 5,10-methylenetetrahydrofolate reductase by phosphorylation and S-adenosylmethionine inhibition.
Froese et al. (2018)
1 more