188.8.131.52: vitamin D 1,25-hydroxylase
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For detailed information about vitamin D 1,25-hydroxylase, go to the full flat file.
CYP105A1, cytochrome P450SU-1, Streptomyces griseolus cytochrome P450SU-1, vitamin D3 dihydroxylase
1.14.15 With reduced iron-sulfur protein as one donor, and incorporation of one atom of oxygen into the other donor
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Crystallization on EC 184.108.40.206 - vitamin D 1,25-hydroxylase
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structure of the mutant R73V/R84A with 1alpha,25-dihydroxyvitamin D3, a hydrogen-bond network including the 1alpha-hydroxyl group and several water molecules play an important role in the substrate-binding for 26-hydroxylation
wild-type to 1.5 A resolution, and mutant R84A, native protein and in complex with 1alpha,25-dihydroxyvitamin D3. The compound is positioned 11 A from the iron atom along the I helix within the pocket. The loss of two hydrogen bonds in the R84A mutant increases the adaptability of the B and F helices, creating a transient binding site