› 4go2

X-ray diffraction
2.28Å resolution

Crystal structure of the c-terminal domain of 10'formyltetrahydrofolate dehydrogenase in complex with Thio-NADP

Released:
DOI: 10.2210/pdb4go2/pdb
PDB entry 4go2 coloured by chain, front view.
PDB entry 4go2 coloured by chain, side view.
PDB entry 4go2 coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.
Tsybovsky Y, Malakhau Y, Strickland KC, Krupenko SA
Chem Biol Interact 202 62-9 (2013)
PMID: 23295222

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: 56.62 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 TAP 4 x TAP
2 bound ligands:
Ligand SO4 28 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 258.935Å b: 194.391Å c: 97.114Å
α: 90° β: 109.02° γ: 90°
R-values:
R R work R free
0.178 0.177 0.196
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Loss of ALDH1L1 folate enzyme confers a selective metabolic advantage for tumor progression.
Krupenko et al. (2019)
1 more

1 mention without citation

The mechanism of discrimination between oxidized and reduced coenzyme in the aldehyde dehydrogenase domain of Aldh1l1.
Tsybovsky et al. (2013)