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Literature summary for 1.3.7.11 extracted from
- Structure and mutation analysis of archaeal geranylgeranyl reductase (2011), J. Mol. Biol., 409, 543-557.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Sulfolobus acidocaldarius |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystals are obtained using 3.5-4.5 M sodium formate with 0.1 M sodium acetate buffer, pH 4.6, as the precipitant solution and 1.0 mM geranylgeranyl diphosphate is added for co-crystallization, 1.8 A resolution | Sulfolobus acidocaldarius |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sulfolobus acidocaldarius | Q4JA33 | - |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | divided into the FADbinding, catalytic and C-terminal domains | Sulfolobus acidocaldarius |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| geranylgeranyl reductase | - |
Sulfolobus acidocaldarius |
| Sa-GGR | - |
Sulfolobus acidocaldarius |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| FAD | flavoprotein, the catalytic domain has a large cavity surrounded by a characteristic YxWxFPx7-8GxG motif and by the isoalloxazine ring of an FAD molecule | Sulfolobus acidocaldarius |  |
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