Literature summary 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.

Cloned(Commentary)

EC Number	Cloned (Comment)	Organism
1.14.13.154	expression in Escherichia coli	Saccharopolyspora erythraea

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.14.13.154	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

EC Number	Organism	UniProt	Comment	Textmining
1.14.13.154	Saccharopolyspora erythraea	P48635	-	-

Synonyms

EC Number	Synonyms	Comment	Organism
1.14.13.154	CYP113A1	-	Saccharopolyspora erythraea

Cofactor

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

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Release 2023.1 (January 2023)