› 3hud

X-ray diffraction
3.2Å resolution

THE STRUCTURE OF HUMAN BETA 1 BETA 1 ALCOHOL DEHYDROGENASE: CATALYTIC EFFECTS OF NON-ACTIVE-SITE SUBSTITUTIONS

Released:
DOI: 10.2210/pdb3hud/pdb
PDB entry 3hud coloured by chain, front view.
PDB entry 3hud coloured by chain, side view.
PDB entry 3hud coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of human beta 1 beta 1 alcohol dehydrogenase: catalytic effects of non-active-site substitutions.
Hurley TD, Bosron WF, Hamilton JA, Amzel LM
Proc Natl Acad Sci U S A 88 8149-53 (1991)
PMID: 1896463

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
1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 54.59Å b: 45.05Å c: 93.86Å
α: 91.93° β: 102.5° γ: 68.82°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Escherichia coli

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Citations

2 review citations

Molecular characterization of microbial alcohol dehydrogenases.
Reid et al. (1994)
1 more

2 mentions without citation

Role of PhaC Type I and Type II Enzymes during PHA Biosynthesis.
Mezzolla et al. (2018)
1 more