› 4r8v

X-ray diffraction
2.2Å resolution

Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with formate

Released:
DOI: 10.2210/pdb4r8v/pdb
PDB entry 4r8v coloured by chain, front view.
PDB entry 4r8v coloured by chain, side view.
PDB entry 4r8v coloured by chain, top view.
Source organism: Danio rerio
Primary publication:
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 CC, Chuankhayan P, Chang WN, Kao TT, Guan HH, Fun HK, Nakagawa A, Fu TF, Chen CJ
Acta Crystallogr D Biol Crystallogr 71 1006-21 (2015)
PMID: 25849409

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122879 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
10-formyltetrahydrofolate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 318 amino acids
Theoretical weight: 35.46 KDa
Source organism: Danio rerio
Expression system: Escherichia coli
UniProt:
  • Canonical: E3NZ06 (Residues: 1-311; Coverage: 34%)
Gene name: aldh1l1
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand BTB 1 x BTB
Ligand PEG 1 x PEG
Ligand FMT 1 x FMT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21212
Unit cell:
a: 103.98Å b: 51.977Å c: 59.936Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.237
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Modeling of interactions between functional domains of ALDH1L1.
Horita et al. (2017)
3 more

1 mention 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)