eF-site ID 6dyy-A PDB Code 6dyy Chain A click to enlarge Title Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-(((3-(1-butyl-1H-1,2,3-triazol-4-yl)propyl)thio)methyl)pyrrolidin-3-ol Classification HYDROLASE/HYDROLASE INHIBITOR Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Source (A0A1W0VQJ9_HELPX) Sequence A:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL Description Functional site 1) chain A residue 123 type sequence T description binding site for residue EDO A 301 source : AC1 2) chain A residue 125 type sequence G description binding site for residue EDO A 301 source : AC1 3) chain A residue 126 type sequence S description binding site for residue EDO A 301 source : AC1 4) chain A residue 229 type sequence E description binding site for residue MG A 302 source : AC2 5) chain A residue 52 type sequence I description binding site for residue OS6 A 303 source : AC3 6) chain A residue 78 type sequence V description binding site for residue OS6 A 303 source : AC3 7) chain A residue 79 type sequence A description binding site for residue OS6 A 303 source : AC3 8) chain A residue 80 type sequence G description binding site for residue OS6 A 303 source : AC3 9) chain A residue 152 type sequence Q description binding site for residue OS6 A 303 source : AC3 10) chain A residue 153 type sequence F description binding site for residue OS6 A 303 source : AC3 11) chain A residue 154 type sequence V description binding site for residue OS6 A 303 source : AC3 12) chain A residue 172 type sequence V description binding site for residue OS6 A 303 source : AC3 13) chain A residue 173 type sequence E description binding site for residue OS6 A 303 source : AC3 14) chain A residue 174 type sequence M description binding site for residue OS6 A 303 source : AC3 15) chain A residue 175 type sequence E description binding site for residue OS6 A 303 source : AC3 16) chain A residue 197 type sequence S description binding site for residue OS6 A 303 source : AC3 17) chain A residue 198 type sequence D description binding site for residue OS6 A 303 source : AC3 18) chain A residue 200 type sequence A description binding site for residue OS6 A 303 source : AC3 19) chain A residue 208 type sequence F description binding site for residue OS6 A 303 source : AC3 20) chain A residue 106 type sequence A description binding site for residue EDO B 302 source : AC5 21) chain A residue 107 type sequence F description binding site for residue EDO B 302 source : AC5 22) chain A residue 104 type sequence L description binding site for residue OS6 B 305 source : AC8 23) chain A residue 109 type sequence H description binding site for residue OS6 B 305 source : AC8 24) chain A residue 115 type sequence P description binding site for residue OS6 B 305 source : AC8 25) chain A residue 157 type sequence K description binding site for residue EDO C 302 source : AD1 26) chain A residue 122 type sequence E description binding site for residue OS6 C 303 source : AD2 27) chain A residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 29) chain A residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 30) chain A residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 31) chain A residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2

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