PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 60-64 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 323-327 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-10 2005 In addition, three-dimensional computerized modeling of the heme-binding site of the P450c17 enzyme indicated that replacement of Arg by Cys at amino acid position 440 predicts a loss of the catalytic activity of the enzyme, as the mutant enzyme containing Cys440 fails to form a hydrogen bond with the propionate group of heme, which renders the mutant enzyme unable to stabilize the proper position of heme. Heme 323-327 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92 16176874-11 2005 Based on these findings we conclude that expressing the CYP17 gene with functional analysis, combined with three-dimensional computerized modeling of the heme-binding site of the protein provide feasible tools for molecular characterizing of functional consequences of the novel CYP17 mutation on enzyme function. Heme 154-158 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 56-61 16176874-11 2005 Based on these findings we conclude that expressing the CYP17 gene with functional analysis, combined with three-dimensional computerized modeling of the heme-binding site of the protein provide feasible tools for molecular characterizing of functional consequences of the novel CYP17 mutation on enzyme function. Heme 154-158 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 279-284