eF-site ID 4bmx-AB PDB Code 4bmx Chain A, B click to enlarge Title Native structure of futalosine hydrolase of Helicobacter pylori strain 26695 Classification HYDROLASE Compound MTA/SAH NUCLEOSIDASE Source Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) (MTNN_HELPY) Sequence A:  HMVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV AGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPESA IFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSKE RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD NSFDAFLEKSAQTSAKFLKSMVDEL B:  SHMVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHK GVYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSG VAGSLVKDLKINDLLVAIQLVQHDVDLSAFDHPLGFIPES AIFIETSESLNALAKEVANEQHIVLKEGVIASGDQFVHSK ERKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSIS DNADEEANMSFDAFLEKSAQTSAKFLKSMVDEL Description Functional site 1) chain B residue 80 type sequence A description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 2) chain B residue 81 type sequence G description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 3) chain B residue 154 type sequence F description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 4) chain B residue 155 type sequence V description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 5) chain B residue 173 type sequence V description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 6) chain B residue 174 type sequence E description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 7) chain B residue 175 type sequence M description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 8) chain B residue 198 type sequence S description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 9) chain B residue 199 type sequence D description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 10) chain B residue 201 type sequence A description BINDING SITE FOR RESIDUE ADE B 1232 source : AC1 11) chain B residue 1 type sequence M description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 12) chain B residue 10 type sequence A description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 13) chain B residue 11 type sequence M description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 14) chain B residue 14 type sequence E description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 15) chain B residue 79 type sequence V description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 16) chain B residue 174 type sequence E description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 17) chain B residue 175 type sequence M description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 18) chain B residue 176 type sequence E description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 19) chain B residue 195 type sequence R description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 20) chain B residue 209 type sequence F description BINDING SITE FOR RESIDUE TRS B 1233 source : AC2 21) chain A residue 125 type sequence S description BINDING SITE FOR RESIDUE TRS A 1232 source : AC3 22) chain A residue 126 type sequence E description BINDING SITE FOR RESIDUE TRS A 1232 source : AC3 23) chain A residue 127 type sequence S description BINDING SITE FOR RESIDUE TRS A 1232 source : AC3 24) chain A residue 14 type ACT_SITE sequence E description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 14 type ACT_SITE sequence E description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 26) chain A residue 199 type ACT_SITE sequence D description Proton donor => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 199 type ACT_SITE sequence D description Proton donor => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 81 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 29) chain A residue 175 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI3 30) chain B residue 81 type BINDING sequence G description source Swiss-Prot : SWS_FT_FI3 31) chain B residue 155 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 32) chain B residue 175 type BINDING sequence M description source Swiss-Prot : SWS_FT_FI3 33) chain A residue 155 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3

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