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EC Number Crystallization (Commentary)
Show all pathways known for 1.3.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.22molecular docking of inhibitors. The furanonaphthoquinones reside closely adjacent to NADPH and likely interact with Tyr95 of the enzyme as well as NADPH
Show all pathways known for 1.3.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.22structure of SRD5A in complex with NADPH at 2.0 A resolution. SRD5A exists as a monomer comprised of seven transmembrane segments (TMs). The TM1-4 enclose a hydrophobic substrate binding cavity, whereas TM5-7 coordinate cofactor NADPH through extensive hydrogen bonds network
Show all pathways known for 1.3.1.22Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.22structure of SRD5A2 with finasteride at 2.8 A, reveals a 7-TM structural topology and an intermediate adduct of finasteride and NADPH as NADP-dihydrofinasteride in a largely enclosed binding cavity inside the transmembrane domain. The molecular mechanisms of the reaction and of finasteride inhibition involve residues E57 and Y91. The cytosolic region that regulates NADPH/NADP+ exchange displays high conformational dynamics
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