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Literature summary for 1.14.13.154 extracted from
- Cloning, expression, purification, crystallization and preliminary X-ray crystallographic analysis of C-12 hydroxylase EryK from Saccharopolyspora erythraea (2008), Protein Pept. Lett., 15, 1138-1141.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Saccharopolyspora erythraea |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| different crystal forms are harvested from distinct crystallization conditions: two ligand-free forms, one substrate bound and two inhibitors-bound. All crystals belong either to the monoclinc P2(1)or to the orthorhombic P2(1)2(1)2(1) space groups, and exhibit diffraction limits ranging from 2.3 to 1.6 A | Saccharopolyspora erythraea |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharopolyspora erythraea | P48635 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CYP113A1 | - |
Saccharopolyspora erythraea |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| cytochrome P-450 | a heme-thiolate protein (P-450) | Saccharopolyspora erythraea |
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