› 3rhj

X-ray diffraction
1.89Å resolution

Crystal structure of the E673A mutant of the C-terminal domain of RAT 10'FORMYLTETRAHYDROFOLATE DEHYDROGENASE in complex with co-purified NADP

Released:
DOI: 10.2210/pdb3rhj/pdb
PDB entry 3rhj coloured by chain, front view.
PDB entry 3rhj coloured by chain, side view.
PDB entry 3rhj coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme.
Tsybovsky Y, Krupenko SA
J Biol Chem 286 23357-67 (2011)
PMID: 21540484

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytosolic 10-formyltetrahydrofolate dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 517 amino acids
Theoretical weight: 56.56 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P28037 (Residues: 397-902; Coverage: 56%)
Gene names: Aldh1l1, Fthfd
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments


Cofactor: Ligand NAP 4 x NAP
2 bound ligands:
Ligand SO4 24 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 259.391Å b: 194.933Å c: 97.48Å
α: 90° β: 108.94° γ: 90°
R-values:
R R work R free
0.189 0.189 0.203
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Aldehyde dehydrogenases: from eye crystallins to metabolic disease and cancer stem cells.
Vasiliou et al. (2013)
2 more

1 mention without citation

Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme.
Tsybovsky et al. (2011)