› 4iom

X-ray diffraction
3Å resolution

N10-formyltetrahydrofolate synthetase from Moorella thermoacetica with folate

Released:
DOI: 10.2210/pdb4iom/pdb
PDB entry 4iom coloured by chain, front view.
PDB entry 4iom coloured by chain, side view.
PDB entry 4iom coloured by chain, top view.
Source organism: Moorella thermoacetica ATCC 39073
Primary publication:
Time passes yet errors remain: comments on the structure of N10-formyltetrahydrofolate synthetase.
Stec B
Protein Sci 22 671-4 (2013)
PMID: 23533144

Function and Biology Details

Reaction catalysed: 
ATP + formate + tetrahydrofolate = ADP + phosphate + 10-formyltetrahydrofolate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173900 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formate--tetrahydrofolate ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 559 amino acids
Theoretical weight: 60.01 KDa
Source organism: Moorella thermoacetica ATCC 39073
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2RM91 (Residues: 1-559; Coverage: 100%)
Gene names: Moth_0109, fhs
Sequence domains: Formate--tetrahydrofolate ligase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SO4 7 x SO4
Ligand TOE 3 x TOE
Ligand FOL 1 x FOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: R32
Unit cell:
a: 160.99Å b: 160.99Å c: 256.61Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.213 0.291
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Resolving the cofactor-binding site in the proline biosynthetic enzyme human pyrroline-5-carboxylate reductase 1.
Christensen et al. (2017)
1 more

1 mention without citation

Time passes yet errors remain: comments on the structure of N10-formyltetrahydrofolate synthetase.
Stec B. (2013)