PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 25251696-5 2014 Molecular docking studies demonstrated quite similar binding patterns of all new pregnenolone derivatives at the active site of CYP17 through hydrogen bonding and hydrophobic interaction. Hydrogen 142-150 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 128-133 34662099-12 2021 The observed switch in substrate specificity of the enzyme is consistent with this result if the hydrogen bonding to the proximal peroxo oxygen is necessary for a proposed nucleophilic peroxoanion-mediated mechanism for CYP17A1 in carbon-carbon bond scission. Hydrogen 97-105 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 220-227 33656879-5 2021 For CYP17A1 with 17OH-PROG, a characteristic shift of the Fe-O mode is observed in the presence of Mn-b5, indicating reorientation of a hydrogen bond between the 17OH group of the substrate from the terminal to the proximal oxygen atom of the Fe-O-O moiety, a configuration favorable for the lyase catalysis. Hydrogen 136-144 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 4-11 30431391-1 2019 According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001). Hydrogen 115-123 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 45-52 30431391-1 2019 According to the X-ray crystal structures of CYP17A1 (including its complexes with inhibitors), it is shown that a hydrogen bond exists between CYP17A1 and its inhibitors (such as abiraterone and TOK-001). Hydrogen 115-123 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 144-151 30431391-4 2019 In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1. Hydrogen 232-240 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 138-145 30431391-4 2019 In the case of abiraterone binding, the unfilled volume in the active site cavity increases the freedom of movement of abiraterone within CYP17A1, leading to the collective motions of the helices G and B" as well as the breaking of hydrogen bond existing between the 3beta-OH group of abiraterone and N202 of CYP17A1. Hydrogen 232-240 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 309-316 29283561-4 2018 Here we show that the identity of the residue at position 202 in human CYP17A1, thought to form a hydrogen bond with the A-ring alcohol substituent on the pregnene- nucleus, is a key driver of this enzyme"s native preference for OHPREG. Hydrogen 98-106 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 71-78 27566228-5 2017 While both hydroxylase and lyase substrates have similar orientations with respect to the heme, subtle differences in hydrogen bonding between CYP17A1 and the C3 substituent at the opposite end of ligands appear to correlate with differential substrate utilization and product formation. Hydrogen 118-126 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 143-150 26682016-6 2015 Considering on the effect of hydrophobic interaction and hydrogen bonding between abiraterone and CYP17A1, the key residues of Phe114, Ile371, Val482, and Asn202 were identified. Hydrogen 57-65 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 98-105 26051784-6 2015 Molecular docking study of 21 was performed and showed the hydrogen bonds and hydrophobic interaction with the amino acid residues of the active site of CYP17. Hydrogen 59-67 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 153-158 12773039-4 2003 Common chemical features in the steroid and nonsteroid human CYP17 enzyme inhibitors, as deduced by the Catalyst/HipHop program, are one to two hydrogen bond acceptors (HBAs) and three hydrophobic groups. Hydrogen 144-152 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 61-66 12773039-6 2003 A model that permits hydrogen bond interaction between the azole functionality on ring D and the enzyme is consistent with experimental deductions for type II CYP17 inhibitors where a sixth ligating atom interacts with Fe(II) of heme. Hydrogen 21-29 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 159-164 31818479-12 2020 Docking simulations discovers hydrogen bonding and hydrophobic interactions as responsible for the binding affinities of hits to the CYP17A1 Protein Data Bank structure. Hydrogen 30-38 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 133-140 28387522-7 2017 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. Hydrogen 28-36 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 94-101 28387522-7 2017 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. Hydrogen 28-36 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 112-119 28387522-7 2017 Finally, differences in the hydrogen-bond pattern of the substrates were detected both in the CYP17A1-Cpd I and CYP17A1-POA complexes, with the former found to be more pivotal for the hydroxylation site than the latter, suggesting a possible explanation for the slower conversion of CYP17A1 for 17alpha-hydroxyprogesterone over 17alpha-hydroxypregnenolone. Hydrogen 28-36 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 112-119 25988615-5 2015 Molecular docking study of 37 showed binding with the amino acid residues of CYP17 through hydrogen bonds and hydrophobic interaction. Hydrogen 91-99 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 77-82 23576395-0 2013 Differential hydrogen bonding in human CYP17 dictates hydroxylation versus lyase chemistry. Hydrogen 13-21 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 39-44 22266943-6 2012 Whereas the overall structure of CYP17A1 provides a rationale for understanding many mutations that are found in patients with steroidogenic diseases, the active site reveals multiple steric and hydrogen bonding features that will facilitate a better understanding of the enzyme"s dual hydroxylase and lyase catalytic capabilities and assist in rational drug design. Hydrogen 195-203 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 33-40 16473871-12 2006 The 3D template also suggested the position of a residue, which could be involved in a hydrogen bond with CYP17 substrates and the shape and location of a cavity. Hydrogen 87-95 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 106-111 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. Hydrogen 280-288 cytochrome P450 family 17 subfamily A member 1 Homo sapiens 85-92