› 2cfi

X-ray diffraction
1.85Å resolution

The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin

Released:
DOI: 10.2210/pdb2cfi/pdb
PDB entry 2cfi coloured by chain, front view.
PDB entry 2cfi coloured by chain, side view.
PDB entry 2cfi coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the hydrolase domain of human 10-formyltetrahydrofolate dehydrogenase and its complex with a substrate analogue.
Kursula P, Schüler H, Flodin S, Nilsson-Ehle P, Ogg DJ, Savitsky P, Nordlund P, Stenmark P
Acta Crystallogr D Biol Crystallogr 62 1294-9 (2006)
PMID: 17057331

Function and Biology Details

Reaction catalysed: 
10-formyltetrahydrofolate + NADP(+) + H(2)O = tetrahydrofolate + CO(2) + NADPH
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131158 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic 10-formyltetrahydrofolate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 329 amino acids
Theoretical weight: 36.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O75891 (Residues: 1-307; Coverage: 34%)
Gene names: ALDH1L1, FTHFD
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand ZZZ 1 x ZZZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 108.14Å b: 64.44Å c: 58.87Å
α: 90° β: 98.79° γ: 90°
R-values:
R R work R free
0.181 0.178 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

FDH: an aldehyde dehydrogenase fusion enzyme in folate metabolism.
Krupenko SA. (2009)
1 more

2 mentions without citation

Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Lin et al. (2015)
1 more