› 2fzw

X-ray diffraction
1.84Å resolution

Structure of the binary complex of the E67L mutant of human glutathione-dependent formaldehyde dehydrogenase with NAD(H)

Released:
DOI: 10.2210/pdb2fzw/pdb
PDB entry 2fzw coloured by chain, front view.
PDB entry 2fzw coloured by chain, side view.
PDB entry 2fzw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-function relationships in human glutathione-dependent formaldehyde dehydrogenase. Role of Glu-67 and Arg-368 in the catalytic mechanism.
Sanghani PC, Davis WI, Zhai L, Robinson H
Biochemistry 45 4819-30 (2006)
PMID: 16605250

Function and Biology Details

Reactions catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
S-(hydroxymethyl)glutathione + NAD(P)(+) = S-formylglutathione + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145918 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase class-3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 373 amino acids
Theoretical weight: 39.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P11766 (Residues: 2-374; Coverage: 100%)
Gene names: ADH5, ADHX, FDH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
3 bound ligands:
Ligand ZN 4 x ZN
Ligand PO4 3 x PO4
Ligand K 2 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P43212
Unit cell:
a: 79.27Å b: 79.27Å c: 311.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.177 0.204
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

Formaldehyde Stress Responses in Bacterial Pathogens.
Chen et al. (2016)
4 more

2 mentions without citation

Computational studies of human class V alcohol dehydrogenase - the odd sibling.
Östberg et al. (2016)
1 more