eF-site ID 6dyy-ABCD PDB Code 6dyy Chain A, B, C, D 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 B:  VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVY HNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAG SLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESAIF IETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKERK EFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNA DEKAGMSFDEFLEKSAHTSAKFLKSMVDEL C:  VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVY HNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAG SLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESAIF IETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKERK EFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNA DEKAGMSFDEFLEKSAHTSAKFLKSMVDEL D:  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 C residue 209 type sequence D description binding site for residue EDO A 301 source : AC1 5) chain D residue 107 type sequence F description binding site for residue EDO A 301 source : AC1 6) chain A residue 229 type sequence E description binding site for residue MG A 302 source : AC2 7) chain A residue 52 type sequence I description binding site for residue OS6 A 303 source : AC3 8) chain A residue 78 type sequence V description binding site for residue OS6 A 303 source : AC3 9) chain A residue 79 type sequence A description binding site for residue OS6 A 303 source : AC3 10) chain A residue 80 type sequence G description binding site for residue OS6 A 303 source : AC3 11) chain A residue 152 type sequence Q description binding site for residue OS6 A 303 source : AC3 12) chain A residue 153 type sequence F description binding site for residue OS6 A 303 source : AC3 13) chain A residue 154 type sequence V description binding site for residue OS6 A 303 source : AC3 14) chain A residue 172 type sequence V description binding site for residue OS6 A 303 source : AC3 15) chain A residue 173 type sequence E description binding site for residue OS6 A 303 source : AC3 16) chain A residue 174 type sequence M description binding site for residue OS6 A 303 source : AC3 17) chain A residue 175 type sequence E description binding site for residue OS6 A 303 source : AC3 18) chain A residue 197 type sequence S description binding site for residue OS6 A 303 source : AC3 19) chain A residue 198 type sequence D description binding site for residue OS6 A 303 source : AC3 20) chain A residue 200 type sequence A description binding site for residue OS6 A 303 source : AC3 21) chain A residue 208 type sequence F description binding site for residue OS6 A 303 source : AC3 22) chain B residue 109 type sequence H description binding site for residue OS6 A 303 source : AC3 23) chain B residue 115 type sequence P description binding site for residue OS6 A 303 source : AC3 24) chain B residue 116 type sequence E description binding site for residue OS6 A 303 source : AC3 25) chain B residue 123 type sequence T description binding site for residue EDO B 301 source : AC4 26) chain B residue 125 type sequence G description binding site for residue EDO B 301 source : AC4 27) chain B residue 126 type sequence S description binding site for residue EDO B 301 source : AC4 28) chain C residue 107 type sequence F description binding site for residue EDO B 301 source : AC4 29) chain D residue 209 type sequence D description binding site for residue EDO B 301 source : AC4 30) chain A residue 106 type sequence A description binding site for residue EDO B 302 source : AC5 31) chain A residue 107 type sequence F description binding site for residue EDO B 302 source : AC5 32) chain B residue 205 type sequence G description binding site for residue EDO B 302 source : AC5 33) chain B residue 206 type sequence M description binding site for residue EDO B 302 source : AC5 34) chain B residue 209 type sequence D description binding site for residue EDO B 302 source : AC5 35) chain B residue 138 type sequence Q description binding site for residue EDO B 303 source : AC6 36) chain B residue 139 type sequence H description binding site for residue EDO B 303 source : AC6 37) chain B residue 165 type sequence S description binding site for residue EDO B 303 source : AC6 38) chain B residue 166 type sequence E description binding site for residue EDO B 303 source : AC6 39) chain B residue 133 type sequence K description binding site for residue MG B 304 source : AC7 40) chain A residue 104 type sequence L description binding site for residue OS6 B 305 source : AC8 41) chain A residue 109 type sequence H description binding site for residue OS6 B 305 source : AC8 42) chain A residue 115 type sequence P description binding site for residue OS6 B 305 source : AC8 43) chain B residue 9 type sequence A description binding site for residue OS6 B 305 source : AC8 44) chain B residue 52 type sequence I description binding site for residue OS6 B 305 source : AC8 45) chain B residue 78 type sequence V description binding site for residue OS6 B 305 source : AC8 46) chain B residue 79 type sequence A description binding site for residue OS6 B 305 source : AC8 47) chain B residue 80 type sequence G description binding site for residue OS6 B 305 source : AC8 48) chain B residue 152 type sequence Q description binding site for residue OS6 B 305 source : AC8 49) chain B residue 153 type sequence F description binding site for residue OS6 B 305 source : AC8 50) chain B residue 154 type sequence V description binding site for residue OS6 B 305 source : AC8 51) chain B residue 172 type sequence V description binding site for residue OS6 B 305 source : AC8 52) chain B residue 173 type sequence E description binding site for residue OS6 B 305 source : AC8 53) chain B residue 174 type sequence M description binding site for residue OS6 B 305 source : AC8 54) chain B residue 175 type sequence E description binding site for residue OS6 B 305 source : AC8 55) chain B residue 197 type sequence S description binding site for residue OS6 B 305 source : AC8 56) chain B residue 198 type sequence D description binding site for residue OS6 B 305 source : AC8 57) chain B residue 208 type sequence F description binding site for residue OS6 B 305 source : AC8 58) chain C residue 132 type sequence K description binding site for residue OS6 B 305 source : AC8 59) chain C residue 32 type sequence G description binding site for residue EDO C 301 source : AC9 60) chain C residue 33 type sequence N description binding site for residue EDO C 301 source : AC9 61) chain C residue 34 type sequence V description binding site for residue EDO C 301 source : AC9 62) chain C residue 49 type sequence Y description binding site for residue EDO C 301 source : AC9 63) chain A residue 157 type sequence K description binding site for residue EDO C 302 source : AD1 64) chain C residue 156 type sequence S description binding site for residue EDO C 302 source : AD1 65) chain C residue 157 type sequence K description binding site for residue EDO C 302 source : AD1 66) chain C residue 201 type sequence D description binding site for residue EDO C 302 source : AD1 67) chain C residue 202 type sequence E description binding site for residue EDO C 302 source : AD1 68) chain A residue 122 type sequence E description binding site for residue OS6 C 303 source : AD2 69) chain C residue 9 type sequence A description binding site for residue OS6 C 303 source : AD2 70) chain C residue 52 type sequence I description binding site for residue OS6 C 303 source : AD2 71) chain C residue 78 type sequence V description binding site for residue OS6 C 303 source : AD2 72) chain C residue 79 type sequence A description binding site for residue OS6 C 303 source : AD2 73) chain C residue 80 type sequence G description binding site for residue OS6 C 303 source : AD2 74) chain C residue 152 type sequence Q description binding site for residue OS6 C 303 source : AD2 75) chain C residue 153 type sequence F description binding site for residue OS6 C 303 source : AD2 76) chain C residue 154 type sequence V description binding site for residue OS6 C 303 source : AD2 77) chain C residue 172 type sequence V description binding site for residue OS6 C 303 source : AD2 78) chain C residue 173 type sequence E description binding site for residue OS6 C 303 source : AD2 79) chain C residue 174 type sequence M description binding site for residue OS6 C 303 source : AD2 80) chain C residue 175 type sequence E description binding site for residue OS6 C 303 source : AD2 81) chain C residue 197 type sequence S description binding site for residue OS6 C 303 source : AD2 82) chain C residue 198 type sequence D description binding site for residue OS6 C 303 source : AD2 83) chain C residue 208 type sequence F description binding site for residue OS6 C 303 source : AD2 84) chain D residue 107 type sequence F description binding site for residue OS6 C 303 source : AD2 85) chain D residue 109 type sequence H description binding site for residue OS6 C 303 source : AD2 86) chain D residue 32 type sequence G description binding site for residue EDO D 301 source : AD3 87) chain D residue 33 type sequence N description binding site for residue EDO D 301 source : AD3 88) chain D residue 34 type sequence V description binding site for residue EDO D 301 source : AD3 89) chain D residue 49 type sequence Y description binding site for residue EDO D 301 source : AD3 90) chain C residue 109 type sequence H description binding site for residue OS6 D 302 source : AD4 91) chain D residue 9 type sequence A description binding site for residue OS6 D 302 source : AD4 92) chain D residue 52 type sequence I description binding site for residue OS6 D 302 source : AD4 93) chain D residue 78 type sequence V description binding site for residue OS6 D 302 source : AD4 94) chain D residue 79 type sequence A description binding site for residue OS6 D 302 source : AD4 95) chain D residue 80 type sequence G description binding site for residue OS6 D 302 source : AD4 96) chain D residue 153 type sequence F description binding site for residue OS6 D 302 source : AD4 97) chain D residue 154 type sequence V description binding site for residue OS6 D 302 source : AD4 98) chain D residue 172 type sequence V description binding site for residue OS6 D 302 source : AD4 99) chain D residue 173 type sequence E description binding site for residue OS6 D 302 source : AD4 100) chain D residue 174 type sequence M description binding site for residue OS6 D 302 source : AD4 101) chain D residue 175 type sequence E description binding site for residue OS6 D 302 source : AD4 102) chain D residue 197 type sequence S description binding site for residue OS6 D 302 source : AD4 103) chain D residue 198 type sequence D description binding site for residue OS6 D 302 source : AD4 104) chain D residue 208 type sequence F description binding site for residue OS6 D 302 source : AD4 105) chain A residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 106) chain B residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 107) chain C residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 108) chain D residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 109) chain A residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2 110) chain B residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2 111) chain C residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2 112) chain D residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2 113) chain A residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 114) chain B residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 115) chain C residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 116) chain D residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 117) chain A residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 118) chain A residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 119) chain B residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 120) chain B residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 121) chain C residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 122) chain C residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 123) chain D residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 124) chain D residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4

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