eF-site ID 6dyy-C PDB Code 6dyy Chain C 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 C:  VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVY HNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAG SLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESAIF IETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKERK EFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNA DEKAGMSFDEFLEKSAHTSAKFLKSMVDEL Description Functional site 1) chain C residue 209 type sequence D description binding site for residue EDO A 301 source : AC1 2) chain C residue 107 type sequence F description binding site for residue EDO B 301 source : AC4 3) chain C residue 132 type sequence K description binding site for residue OS6 B 305 source : AC8 4) chain C residue 32 type sequence G description binding site for residue EDO C 301 source : AC9 5) chain C residue 33 type sequence N description binding site for residue EDO C 301 source : AC9 6) chain C residue 34 type sequence V description binding site for residue EDO C 301 source : AC9 7) chain C residue 49 type sequence Y description binding site for residue EDO C 301 source : AC9 8) chain C residue 156 type sequence S description binding site for residue EDO C 302 source : AD1 9) chain C residue 157 type sequence K description binding site for residue EDO C 302 source : AD1 10) chain C residue 201 type sequence D description binding site for residue EDO C 302 source : AD1 11) chain C residue 202 type sequence E description binding site for residue EDO C 302 source : AD1 12) chain C residue 9 type sequence A description binding site for residue OS6 C 303 source : AD2 13) chain C residue 52 type sequence I description binding site for residue OS6 C 303 source : AD2 14) chain C residue 78 type sequence V description binding site for residue OS6 C 303 source : AD2 15) chain C residue 79 type sequence A description binding site for residue OS6 C 303 source : AD2 16) chain C residue 80 type sequence G description binding site for residue OS6 C 303 source : AD2 17) chain C residue 152 type sequence Q description binding site for residue OS6 C 303 source : AD2 18) chain C residue 153 type sequence F description binding site for residue OS6 C 303 source : AD2 19) chain C residue 154 type sequence V description binding site for residue OS6 C 303 source : AD2 20) chain C residue 172 type sequence V description binding site for residue OS6 C 303 source : AD2 21) chain C residue 173 type sequence E description binding site for residue OS6 C 303 source : AD2 22) chain C residue 174 type sequence M description binding site for residue OS6 C 303 source : AD2 23) chain C residue 175 type sequence E description binding site for residue OS6 C 303 source : AD2 24) chain C residue 197 type sequence S description binding site for residue OS6 C 303 source : AD2 25) chain C residue 198 type sequence D description binding site for residue OS6 C 303 source : AD2 26) chain C residue 208 type sequence F description binding site for residue OS6 C 303 source : AD2 27) chain C residue 109 type sequence H description binding site for residue OS6 D 302 source : AD4 28) chain C residue 80 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 29) chain C residue 154 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI4 30) chain C residue 174 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI4 31) chain C residue 13 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI1 32) chain C residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000305|PubMed:20954236 source Swiss-Prot : SWS_FT_FI2

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