› 1m6h

X-ray diffraction
2Å resolution

Human glutathione-dependent formaldehyde dehydrogenase

Released:
DOI: 10.2210/pdb1m6h/pdb
PDB entry 1m6h coloured by chain, front view.
PDB entry 1m6h coloured by chain, side view.
PDB entry 1m6h coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human glutathione-dependent formaldehyde dehydrogenase. Structures of apo, binary, and inhibitory ternary complexes.
Sanghani PC, Robinson H, Bosron WF, Hurley TD
Biochemistry 41 10778-86 (2002)
PMID: 12196016

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: 39.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11766 (Residues: 2-374; Coverage: 100%)
Gene names: ADH5, ADHX, FDH
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand K 2 x K
Ligand PO4 5 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P43212
Unit cell:
a: 78.62Å b: 78.62Å c: 309.659Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.218
Expression system: Escherichia coli

Quick links

Citations

2 review citations

S-Nitrosoglutathione Reductase-The Master Regulator of Protein S-Nitrosation in Plant NO Signaling.
Jahnová et al. (2019)
1 more

6 mentions without citation

S-Nitrosation of Conserved Cysteines Modulates Activity and Stability of S-Nitrosoglutathione Reductase (GSNOR).
Guerra et al. (2016)
5 more