› 2o2p

X-ray diffraction
1.7Å resolution

Crystal structure of the C-terminal domain of rat 10'formyltetrahydrofolate dehydrogenase

Released:
DOI: 10.2210/pdb2o2p/pdb
PDB entry 2o2p coloured by chain, front view.
PDB entry 2o2p coloured by chain, side view.
PDB entry 2o2p coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases.
Tsybovsky Y, Donato H, Krupenko NI, Davies C, Krupenko SA
Biochemistry 46 2917-29 (2007)
PMID: 17302434

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

Assemblies composition:
homo tetramer (preferred)
homo octamer
Assembly name:
PDBe Complex ID:
PDB-CPX-541646 (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 BL21
UniProt:
  • Canonical: P28037 (Residues: 395-902; Coverage: 56%)
Gene names: Aldh1l1, Fthfd
Sequence domains: Aldehyde dehydrogenase family
Structure domains:

Ligands and Environments

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: APS BEAMLINE 22-ID
Spacegroup: C2
Unit cell:
a: 259.5Å b: 194.4Å c: 97.3Å
α: 90° β: 108.9° γ: 90°
R-values:
R R work R free
0.175 0.174 0.189
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Non-P450 aldehyde oxidizing enzymes: the aldehyde dehydrogenase superfamily.
Marchitti et al. (2008)
5 more

7 mentions without citation

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