› 1hdx

X-ray diffraction
2.5Å resolution

THREE-DIMENSIONAL STRUCTURES OF THREE HUMAN ALCOHOL DEHYDROGENASE VARIANTS: CORRELATIONS WITH THEIR FUNCTIONAL DIFFERENCES

Released:
DOI: 10.2210/pdb1hdx/pdb
PDB entry 1hdx coloured by chain, front view.
PDB entry 1hdx coloured by chain, side view.
PDB entry 1hdx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of three human beta alcohol dehydrogenase variants. Correlations with their functional differences.
Hurley TD, Bosron WF, Stone CL, Amzel LM
J Mol Biol 239 415-29 (1994)
PMID: 8201622

Function and Biology Details

Reaction catalysed: 
All-trans-retinol-[cellular-retinol-binding-protein] + NAD(+) = all-trans-retinal-[cellular-retinol-binding-protein] + NADH
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-132402 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
All-trans-retinol dehydrogenase [NAD(+)] ADH1B 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: P00325 (Residues: 2-375; Coverage: 100%)
Gene names: ADH1B, ADH2
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
3 bound ligands:
Ligand ZN 4 x ZN
Ligand CXL 2 x CXL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 54.58Å b: 44.94Å c: 94.3Å
α: 92.29° β: 103.37° γ: 68.97°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Families of retinoid dehydrogenases regulating vitamin A function: production of visual pigment and retinoic acid.
Duester G. (2000)
7 more

6 mentions without citation

Targeting Metalloenzymes for Therapeutic Intervention.
Chen et al. (2019)
5 more