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PDBe Entry: 1h39 
STRUCTURES OF HUMAN OXIDOSQUALENE CYCLASE INHIBITORS BOUND TO A HOMOLGOUS ENZYME
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ISOMERASE
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X-RAY DIFFRACTION
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Resolution: 2.8 Å, R-factor: 22.5%, Free R-factor: 25.5%, Spacegroup: P 32 2 1
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21/08/2003, deposition: 24/08/2002, last revision: 24/02/2009
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Lenhart, A. ; Reinert, D.J. ; Weihofen, W.A. ; Aebi, J.D. ; Dehmlow, H. ; Morand, O.H. ; Schulz, G.E.
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Binding Structures and Potencies of Oxidosqualene Cyclase Inhibitors with the Homologous Squalene-Hopene Cyclase J.MED.CHEM. vol:46, pag:2083 (2003) [PubMed ID 12747780 ]
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ISOMERASE , CHOLESTEROL BIOSYNTHESIS , INHIBITOR , INTERACTIONS , OXIDOSQUALENE CYCLASE , MONOTOPIC MEMBRANE PROTEIN
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5.4.99.17 ExPASy BRENDA (A B C)
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Alicyclobacillus acidocaldarius 405212 (A B C)
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Squalene--hopene cyclase (EC 5.4.99.17) P33247 (A B C)
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A, B, C
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1gsz, 1h35, 1h36, 1h37, 1h3a, 1h3b, 1h3c, 1sqc, 2sqc, 3sqc
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| A, B, C |
SQUALENE--HOPENE CYCLASE |
Protein |
P33247 (SQHC_ALIAD)
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631 |
98% |
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| A, B, C |
(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE |
C8E
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| A, B, C |
ALLYL-{6-[3-(4-BROMO-PHENYL)-1-METHYL-1H-INDAZOL-6-YL]OXY}HEXYL)-N-METHYLAMINE |
R03
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