› 1mc5

X-ray diffraction
2.6Å resolution

Ternary complex of Human glutathione-dependent formaldehyde dehydrogenase with S-(hydroxymethyl)glutathione and NADH

Released:
DOI: 10.2210/pdb1mc5/pdb
PDB entry 1mc5 coloured by chain, front view.
PDB entry 1mc5 coloured by chain, side view.
PDB entry 1mc5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human glutathione-dependent formaldehyde dehydrogenase. Structural changes associated with ternary complex formation.
Sanghani PC, Bosron WF, Hurley TD
Biochemistry 41 15189-94 (2002)
PMID: 12484756

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: 374 amino acids
Theoretical weight: 39.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11766 (Residues: 1-374; Coverage: 100%)
Gene names: ADH5, ADHX, FDH
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
4 bound ligands:
Ligand ZN 4 x ZN
Ligand K 1 x K
Ligand PO4 3 x PO4
Ligand AHE 1 x AHE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 78.656Å b: 78.656Å c: 311.428Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.197 0.249
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Conformational changes and catalysis by alcohol dehydrogenase.
Plapp BV. (2010)
4 more

7 mentions without citation

Zinc-binding cysteines: diverse functions and structural motifs.
Pace et al. (2014)
6 more