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EC Number	Crystallization (Commentary)
1.14.14.24	homology modeling. The relative position of Val391 in the beta3a-strand of a homology model and the crystal structure of rat CYP24A1 are consistent with hydrophobic contact of Val391 and the substrate side chain near C21
1.14.14.24	in complex with vitamin D3, to 1.0 A resolution. The CYP2R1 structure adopts a closed conformation with the substrate access channel being covered by the ordered B'-helix and slightly opened to the surface, which defines the substrate entrance point. The active site is lined by conserved, mostly hydrophobic residues. Vitamin D3 is bound in an elongated conformation with the aliphatic side-chain pointing toward the heme. The structure reveals the secosteroid binding mode in an extended active site

EC Number

Crystallization (Commentary)

1.14.14.24

homology modeling. The relative position of Val391 in the beta3a-strand of a homology model and the crystal structure of rat CYP24A1 are consistent with hydrophobic contact of Val391 and the substrate side chain near C21

1.14.14.24

in complex with vitamin D3, to 1.0 A resolution. The CYP2R1 structure adopts a closed conformation with the substrate access channel being covered by the ordered B'-helix and slightly opened to the surface, which defines the substrate entrance point. The active site is lined by conserved, mostly hydrophobic residues. Vitamin D3 is bound in an elongated conformation with the aliphatic side-chain pointing toward the heme. The structure reveals the secosteroid binding mode in an extended active site

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Release 2023.1 (January 2023)