› 3owo

X-ray diffraction
2.07Å resolution

Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 with and without NAD cofactor

Released:
DOI: 10.2210/pdb3owo/pdb
PDB entry 3owo coloured by chain, front view.
PDB entry 3owo coloured by chain, side view.
PDB entry 3owo coloured by chain, top view.
Source organism: Zymomonas mobilis
Primary publication:
Structures of iron-dependent alcohol dehydrogenase 2 from Zymomonas mobilis ZM4 with and without NAD+ cofactor.
Moon JH, Lee HJ, Park SY, Song JM, Park MY, Park HM, Sun J, Park JH, Kim BY, Kim JS
J Mol Biol 407 413-24 (2011)
PMID: 21295587

Function and Biology Details

Reaction catalysed: 
A primary alcohol + NAD(+) = an aldehyde + NADH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143583 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alcohol dehydrogenase 2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 383 amino acids
Theoretical weight: 40.19 KDa
Source organism: Zymomonas mobilis
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DJA2 (Residues: 1-383; Coverage: 100%)
Gene names: ZMO1596, adhB
Sequence domains: Iron-containing alcohol dehydrogenase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FE2 4 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 6C1
Spacegroup: P21
Unit cell:
a: 60.917Å b: 87.51Å c: 124.708Å
α: 90° β: 94.7° γ: 90°
R-values:
R R work R free
0.202 0.202 0.253
Expression system: Escherichia coli

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Citations

20 citation in other articles

The PduQ enzyme is an alcohol dehydrogenase used to recycle NAD+ internally within the Pdu microcompartment of Salmonella enterica.
Cheng et al. (2012)
19 more

2 mentions without citation

Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase.
Carbone et al. (2015)
1 more