Crystallization (Comment) | Organism |
---|---|
ADH-GS, 10 mg/ml protein in 100 mM sodium acetate buffer, pH 4.5, 0.34 mM n-dodecyl-beta-D-maltoside or 0.16 mM C12E8 and either 150 mM ammonium sulfate/6% PEG 3350 or 1.3 M ammonium sulfate only, with or without 2 mM Ca2+, X-ray diffraction structure determination and analysis at 3.0-5.0 A resolution, heavy atom labeling | Gluconobacter oxydans |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | associated, ADH-GS | Gluconobacter oxydans | 16020 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | - |
Gluconobacter oxydans |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gluconobacter oxydans | - |
- |
- |
Subunits | Comment | Organism |
---|---|---|
trimer | heterotrimer with unequal numers of heme groups, overview | Gluconobacter oxydans |
Synonyms | Comment | Organism |
---|---|---|
ADH-GS | - |
Gluconobacter oxydans |
ADH-IIB | - |
- |
More | the enzyme is a type III ADH | Gluconobacter oxydans |
quinocytochrome alcohol dehydrogenase GS | - |
Gluconobacter oxydans |
quinocytochrome alcohol dehydrogenase IIB | - |
- |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
cytochrome | - |
Gluconobacter oxydans | |
heme | 4 molecules per enzyme molecule | Gluconobacter oxydans | |
pyrroloquinoline quinone | dependent on, 1 molecule per enzyme molecule | Gluconobacter oxydans |