eF-site ID 6dyu-AB PDB Code 6dyu Chain A, B 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-((prop-2-yn-1-ylthio)methyl)pyrrolidin-3-ol Classification HYDROLASE Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Source (A0A1W0VQJ9_HELPX) Sequence A:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL B:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL Description Functional site 1) chain A residue 103 type sequence D description binding site for residue EDO A 301 source : AC1 2) chain A residue 152 type sequence Q description binding site for residue EDO A 301 source : AC1 3) chain A residue 153 type sequence F description binding site for residue EDO A 301 source : AC1 4) chain A residue 9 type sequence A description binding site for residue OS2 A 302 source : AC2 5) chain A residue 52 type sequence I description binding site for residue OS2 A 302 source : AC2 6) chain A residue 78 type sequence V description binding site for residue OS2 A 302 source : AC2 7) chain A residue 79 type sequence A description binding site for residue OS2 A 302 source : AC2 8) chain A residue 80 type sequence G description binding site for residue OS2 A 302 source : AC2 9) chain A residue 104 type sequence L description binding site for residue OS2 A 302 source : AC2 10) chain A residue 109 type sequence H description binding site for residue OS2 A 302 source : AC2 11) chain A residue 152 type sequence Q description binding site for residue OS2 A 302 source : AC2 12) chain A residue 153 type sequence F description binding site for residue OS2 A 302 source : AC2 13) chain A residue 154 type sequence V description binding site for residue OS2 A 302 source : AC2 14) chain A residue 172 type sequence V description binding site for residue OS2 A 302 source : AC2 15) chain A residue 173 type sequence E description binding site for residue OS2 A 302 source : AC2 16) chain A residue 174 type sequence M description binding site for residue OS2 A 302 source : AC2 17) chain A residue 175 type sequence E description binding site for residue OS2 A 302 source : AC2 18) chain A residue 197 type sequence S description binding site for residue OS2 A 302 source : AC2 19) chain A residue 198 type sequence D description binding site for residue OS2 A 302 source : AC2 20) chain A residue 200 type sequence A description binding site for residue OS2 A 302 source : AC2 21) chain A residue 208 type sequence F description binding site for residue OS2 A 302 source : AC2 22) chain A residue 54 type sequence K description binding site for residue NH4 A 303 source : AC3 23) chain A residue 54 type sequence K description binding site for residue NH4 A 303 source : AC3 24) chain A residue 101 type sequence D description binding site for residue NH4 A 303 source : AC3 25) chain A residue 101 type sequence D description binding site for residue NH4 A 303 source : AC3 26) chain A residue 151 type sequence D description binding site for residue NH4 A 303 source : AC3 27) chain A residue 151 type sequence D description binding site for residue NH4 A 303 source : AC3 28) chain B residue 122 type sequence E description binding site for residue EDO B 301 source : AC4 29) chain B residue 123 type sequence T description binding site for residue EDO B 301 source : AC4 30) chain B residue 124 type sequence S description binding site for residue EDO B 301 source : AC4 31) chain B residue 184 type sequence Q description binding site for residue EDO B 301 source : AC4 32) chain B residue 188 type sequence V description binding site for residue EDO B 301 source : AC4 33) chain B residue 189 type sequence P description binding site for residue EDO B 301 source : AC4 34) chain B residue 190 type sequence C description binding site for residue EDO B 301 source : AC4 35) chain A residue 187 type sequence G description binding site for residue EDO B 302 source : AC5 36) chain A residue 126 type sequence S description binding site for residue EDO B 303 source : AC6 37) chain A residue 129 type sequence A description binding site for residue EDO B 303 source : AC6 38) chain A residue 130 type sequence L description binding site for residue EDO B 303 source : AC6 39) chain B residue 106 type sequence A description binding site for residue EDO B 303 source : AC6 40) chain B residue 206 type sequence M description binding site for residue EDO B 303 source : AC6 41) chain B residue 159 type sequence R description binding site for residue EDO B 304 source : AC7 42) chain B residue 32 type sequence G description binding site for residue EDO B 305 source : AC8 43) chain B residue 33 type sequence N description binding site for residue EDO B 305 source : AC8 44) chain B residue 34 type sequence V description binding site for residue EDO B 305 source : AC8 45) chain B residue 49 type sequence Y description binding site for residue EDO B 305 source : AC8 46) chain B residue 10 type sequence M description binding site for residue EDO B 307 source : AD1 47) chain B residue 107 type sequence F description binding site for residue EDO B 307 source : AD1 48) chain B residue 209 type sequence D description binding site for residue EDO B 307 source : AD1 49) chain B residue 213 type sequence E description binding site for residue EDO B 308 source : AD2 50) chain B residue 9 type sequence A description binding site for residue OS2 B 309 source : AD3 51) chain B residue 52 type sequence I description binding site for residue OS2 B 309 source : AD3 52) chain B residue 78 type sequence V description binding site for residue OS2 B 309 source : AD3 53) chain B residue 79 type sequence A description binding site for residue OS2 B 309 source : AD3 54) chain B residue 80 type sequence G description binding site for residue OS2 B 309 source : AD3 55) chain B residue 104 type sequence L description binding site for residue OS2 B 309 source : AD3 56) chain B residue 109 type sequence H description binding site for residue OS2 B 309 source : AD3 57) chain B residue 153 type sequence F description binding site for residue OS2 B 309 source : AD3 58) chain B residue 154 type sequence V description binding site for residue OS2 B 309 source : AD3 59) chain B residue 172 type sequence V description binding site for residue OS2 B 309 source : AD3 60) chain B residue 173 type sequence E description binding site for residue OS2 B 309 source : AD3 61) chain B residue 174 type sequence M description binding site for residue OS2 B 309 source : AD3 62) chain B residue 175 type sequence E description binding site for residue OS2 B 309 source : AD3 63) chain B residue 197 type sequence S description binding site for residue OS2 B 309 source : AD3 64) chain B residue 198 type sequence D description binding site for residue OS2 B 309 source : AD3 65) chain B residue 208 type sequence F description binding site for residue OS2 B 309 source : AD3 66) chain B residue 54 type sequence K description binding site for residue NH4 B 310 source : AD4 67) chain B residue 54 type sequence K description binding site for residue NH4 B 310 source : AD4 68) chain B residue 101 type sequence D description binding site for residue NH4 B 310 source : AD4 69) chain B residue 101 type sequence D description binding site for residue NH4 B 310 source : AD4 70) chain B residue 151 type sequence D description binding site for residue NH4 B 310 source : AD4 71) chain B residue 151 type sequence D description binding site for residue NH4 B 310 source : AD4 72) chain A residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 73) chain B residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 74) chain A residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 75) chain B residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 76) chain A residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 77) chain A residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 78) chain B residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 79) chain B residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 80) chain A residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2 81) chain B residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2

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