Literature summary for 1.14.15.35 extracted from

Cupp-Vickery, J.R.; Poulos, T.L.
Structure of cytochrome P450eryF: substrate, inhibitors, and model compounds bound in the active site (1997), Steroids, 62, 112-116.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
modeling of the substrate-binding pocket with ketoconazole bound shos that the secondary nitrogen of the azole ring is coordinated to the heme iron, and nearby regions are positioned in the active site similarly to 6-deoxyerythronolide B, the remainder of the molecule extends into the active site pocket, which is occupied by water in the 6-deoxyerythronolide B complex. The large water-binding pocket in the P450eryF active site appears to provide flexibility in substrate binding and allows for molecules that are larger than 6-deoxyerythronolide B to be accommodated in the active site	Saccharopolyspora erythraea

Crystallization (Comment)

Organism

modeling of the substrate-binding pocket with ketoconazole bound shos that the secondary nitrogen of the azole ring is coordinated to the heme iron, and nearby regions are positioned in the active site similarly to 6-deoxyerythronolide B, the remainder of the molecule extends into the active site pocket, which is occupied by water in the 6-deoxyerythronolide B complex. The large water-binding pocket in the P450eryF active site appears to provide flexibility in substrate binding and allows for molecules that are larger than 6-deoxyerythronolide B to be accommodated in the active site

Saccharopolyspora erythraea

Protein Variants

Protein Variants	Comment	Organism
A245S	about 10fold decrease in affinity for 6-deoxyerythronolide B, and 6fold decrease in specific affinity	Saccharopolyspora erythraea
A245T	about 10fold decrease in affinity for 6-deoxyerythronolide B, and 1000fold decrease in specific affinity	Saccharopolyspora erythraea

Organism

Organism	UniProt	Comment	Textmining
Saccharopolyspora erythraea	-	-	-

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Release 2023.1 (January 2023)