1hdz

X-ray diffraction
2.5Å resolution

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

Released:

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:

Structure analysis Details

Assembly composition:
homo dimer (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: 39.67 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
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 53.56Å b: 44.26Å c: 93.01Å
α: 92.36° β: 103.63° γ: 68.84°
R-values:
R R work R free
0.194 0.194 not available
Expression system: Escherichia coli