› 4qpc

X-ray diffraction
1.9Å resolution

Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (Y200A) from zebrafish

Released:
DOI: 10.2210/pdb4qpc/pdb
PDB entry 4qpc coloured by chain, front view.
PDB entry 4qpc coloured by chain, side view.
PDB entry 4qpc 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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 35.36 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 104.46Å b: 53.959Å c: 60.877Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.204 0.225
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)