eF-site ID 6ayo-B PDB Code 6ayo Chain B click to enlarge Title Crystal structure of Campylobacter jejuni 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with 5'-deoxy-5'-Propyl-DADMe-Immucillin-A Classification HYDROLASE, TRANSFERASE Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Source (A0A1E7P7U4_CAMJU) Sequence B:  GMKIAILGAMSEEITPLLETLKDYTKIEHANNTYYFAKYK DHELVLAYSKIGKVNSTLSASVMIEKFGAQVLLFTGVAGA FNPELEIGDLLYATKLAQYDLDITAFGHPLGFVPGNEIFI KTDEKLNNLALEVAKELNIKLRAGIIATGDEFICDEAKKA KIREIFNADACEMEGASVALVCDALKVPCFILRAMSDKAG EKAEFDFDEFVINSAKISANFVLKMCEKL Description Functional site 1) chain B residue 8 type sequence A description binding site for residue C1Y B 301 source : AC3 2) chain B residue 50 type sequence I description binding site for residue C1Y B 301 source : AC3 3) chain B residue 76 type sequence V description binding site for residue C1Y B 301 source : AC3 4) chain B residue 77 type sequence A description binding site for residue C1Y B 301 source : AC3 5) chain B residue 78 type sequence G description binding site for residue C1Y B 301 source : AC3 6) chain B residue 150 type sequence E description binding site for residue C1Y B 301 source : AC3 7) chain B residue 151 type sequence F description binding site for residue C1Y B 301 source : AC3 8) chain B residue 152 type sequence I description binding site for residue C1Y B 301 source : AC3 9) chain B residue 170 type sequence C description binding site for residue C1Y B 301 source : AC3 10) chain B residue 171 type sequence E description binding site for residue C1Y B 301 source : AC3 11) chain B residue 172 type sequence M description binding site for residue C1Y B 301 source : AC3 12) chain B residue 173 type sequence E description binding site for residue C1Y B 301 source : AC3 13) chain B residue 195 type sequence S description binding site for residue C1Y B 301 source : AC3 14) chain B residue 196 type sequence D description binding site for residue C1Y B 301 source : AC3 15) chain B residue 206 type sequence F description binding site for residue C1Y B 301 source : AC3 16) chain B residue 97 type sequence Q description binding site for residue EDO B 302 source : AC4 17) chain B residue 116 type sequence E description binding site for residue EDO B 302 source : AC4 18) chain B residue 117 type sequence I description binding site for residue EDO B 302 source : AC4 19) chain B residue 119 type sequence I description binding site for residue EDO B 302 source : AC4 20) chain B residue 179 type sequence L description binding site for residue EDO B 302 source : AC4 21) chain B residue 116 type sequence E description binding site for residue EDO B 303 source : AC5 22) chain B residue 117 type sequence I description binding site for residue EDO B 303 source : AC5 23) chain B residue 118 type sequence F description binding site for residue EDO B 303 source : AC5 24) chain B residue 47 type sequence Y description binding site for residue EDO B 304 source : AC6 25) chain B residue 111 type sequence F description binding site for residue EDO B 304 source : AC6 26) chain B residue 116 type sequence E description binding site for residue EDO B 304 source : AC6 27) chain B residue 27 type sequence E description binding site for residue BTB B 305 source : AC7 28) chain B residue 30 type sequence N description binding site for residue BTB B 305 source : AC7 29) chain B residue 31 type sequence N description binding site for residue BTB B 305 source : AC7 30) chain B residue 32 type sequence T description binding site for residue BTB B 305 source : AC7 31) chain B residue 47 type sequence Y description binding site for residue BTB B 305 source : AC7 32) chain B residue 49 type sequence K description binding site for residue BTB B 305 source : AC7 33) chain B residue 114 type sequence G description binding site for residue BTB B 305 source : AC7 34) chain B residue 115 type sequence N description binding site for residue BTB B 305 source : AC7 35) chain B residue 12 type ACT_SITE sequence E description Proton acceptor => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 36) chain B residue 196 type ACT_SITE sequence D description Proton donor => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 78 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 38) chain B residue 152 type BINDING sequence I description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 39) chain B residue 172 type BINDING sequence M description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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