› 1zp3

X-ray diffraction
1.85Å resolution

E. coli Methylenetetrahydrofolate Reductase (oxidized)

Released:
DOI: 10.2210/pdb1zp3/pdb
PDB entry 1zp3 coloured by chain, front view.
PDB entry 1zp3 coloured by chain, side view.
PDB entry 1zp3 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of NADH and CH3-H4folate complexes of Escherichia coli methylenetetrahydrofolate reductase reveal a spartan strategy for a ping-pong reaction.
Pejchal R, Sargeant R, Ludwig ML
Biochemistry 44 11447-57 (2005)
PMID: 16114881

Function and Biology Details

Reaction catalysed: 
5-methyltetrahydrofolate + NAD(+) = 5,10-methylenetetrahydrofolate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142675 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
5,10-methylenetetrahydrofolate reductase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 304 amino acids
Theoretical weight: 34.22 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEZ1 (Residues: 1-296; Coverage: 100%)
Gene names: JW3913, b3941, metF
Sequence domains: Methylenetetrahydrofolate reductase
Structure domains: TIM Barrel

Ligands and Environments

3 bound ligands:
Ligand SO4 4 x SO4
Ligand FAD 3 x FAD
Ligand MPD 3 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 103.236Å b: 127.789Å c: 97.703Å
α: 90° β: 121.55° γ: 90°
R-values:
R R work R free
0.229 0.214 0.237
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Flavin-dependent enzymes in cancer prevention.
Wojcieszyńska et al. (2012)
20 other articles

3 mentions without citation

Evidence for a hexaheteromeric methylenetetrahydrofolate reductase in Moorella thermoacetica.
Mock et al. (2014)
2 more