PDBe 1fp7

X-ray diffraction
3.2Å resolution

MONOVALENT CATION BINDING SITES IN N10-FORMYLTETRAHYDROFOLATE SYNTHETASE FROM MOORELLA THERMOACETICA

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Formate--tetrahydrofolate ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 557 amino acids
Theoretical weight: 59.84 KDa
Source organism: Moorella thermoacetica
Expression system: Escherichia coli
UniProt:
  • Canonical: P21164 (Residues: 1-559; Coverage: 100%)
Gene name: fhs
Sequence domains: Formate--tetrahydrofolate ligase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: R32
Unit cell:
a: 160.876Å b: 160.876Å c: 256.118Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.285 0.285 0.355
Expression system: Escherichia coli