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Literature summary for extracted from

  • Savino, C.; Sciara, G.; Miele, A.E.; Kendrew, S.G., Vallone, B.
    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.
    View publication on PubMed


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 UniProt Comment Textmining
Saccharopolyspora erythraea P48635


Synonyms Comment Organism
Saccharopolyspora erythraea


Cofactor Comment Organism Structure
cytochrome P-450 a heme-thiolate protein (P-450) Saccharopolyspora erythraea