eF-site ID 6if8-ABCD PDB Code 6if8 Chain A, B, C, D click to enlarge Title Aeromonas hydrophila MtaN-2 complexed with adenine Classification HYDROLASE Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase Source (MTNN_AERHH) Sequence A:  AMDPEFMKVGIIGAMEQEVALLRSQMSNPTTLQLGGCEFY QGTLAGKEVILTRSGIGKVAASVATSLLLEKFAPDCVINT GSAGGFAQDLHIGDVVIASEMRFHDVDVTAFGYEMGQMAQ QPAAFPCDETLIAVAQDCKVGLICTGDQFMCKPDAIAKAR ADFPQMLAVEMEGAAIGQVCHMFKVPYLVVRAMSDIAGKE QVESFDAFIEVAGKHSAEVIIKMLGKL B:  GAMDPEFMKVGIIGAMEQEVALLRSQMSNPTTLQLGGCEF YQGTLAGKEVILTRSGIGKVAASVATSLLLEKFAPDCVIN TGSAGGFAQDLHIGDVVIASEMRFHDVDVTAFGYEMGQMA QQPAAFPCDETLIAVAQDCKVGLICTGDQFMCKPDAIAKA RADFPQMLAVEMEGAAIGQVCHMFKVPYLVVRAMSDIAGK EQVESFDAFIEVAGKHSAEVIIKMLGKL C:  AMDPEFMKVGIIGAMEQEVALLRSQMSNPTTLQLGGCEFY QGTLAGKEVILTRSGIGKVAASVATSLLLEKFAPDCVINT GSAGGFAQDLHIGDVVIASEMRFHDVDVTAFGYEMGQMAQ QPAAFPCDETLIAVAQDCKVGLICTGDQFMCKPDAIAKAR ADFPQMLAVEMEGAAIGQVCHMFKVPYLVVRAMSDIAGKE QVESFDAFIEVAGKHSAEVIIKMLGKL D:  GAMDPEFMKVGIIGAMEQEVALLRSQMSNPTTLQLGGCEF YQGTLAGKEVILTRSGIGKVAASVATSLLLEKFAPDCVIN TGSAGGFAQDLHIGDVVIASEMRFHDVDVTAFGYEMGQMA QQPAAFPCDETLIAVAQDCKVGLICTGDQFMCKPDAIAKA RADFPQMLAVEMEGAAIGQVCHMFKVPYLVVRAMSDIAGK EQVESFDAFIEVAGKHSAEVIIKMLGKL Description Functional site 1) chain A residue 77 type sequence A description binding site for residue ADE A 300 source : AC1 2) chain A residue 78 type sequence G description binding site for residue ADE A 300 source : AC1 3) chain A residue 151 type sequence Q description binding site for residue ADE A 300 source : AC1 4) chain A residue 152 type sequence F description binding site for residue ADE A 300 source : AC1 5) chain A residue 153 type sequence M description binding site for residue ADE A 300 source : AC1 6) chain A residue 172 type sequence V description binding site for residue ADE A 300 source : AC1 7) chain A residue 173 type sequence E description binding site for residue ADE A 300 source : AC1 8) chain A residue 174 type sequence M description binding site for residue ADE A 300 source : AC1 9) chain A residue 197 type sequence S description binding site for residue ADE A 300 source : AC1 10) chain A residue 198 type sequence D description binding site for residue ADE A 300 source : AC1 11) chain A residue 204 type sequence Q description binding site for residue ADE A 300 source : AC1 12) chain B residue 77 type sequence A description binding site for residue ADE B 301 source : AC2 13) chain B residue 78 type sequence G description binding site for residue ADE B 301 source : AC2 14) chain B residue 151 type sequence Q description binding site for residue ADE B 301 source : AC2 15) chain B residue 152 type sequence F description binding site for residue ADE B 301 source : AC2 16) chain B residue 153 type sequence M description binding site for residue ADE B 301 source : AC2 17) chain B residue 172 type sequence V description binding site for residue ADE B 301 source : AC2 18) chain B residue 173 type sequence E description binding site for residue ADE B 301 source : AC2 19) chain B residue 174 type sequence M description binding site for residue ADE B 301 source : AC2 20) chain B residue 197 type sequence S description binding site for residue ADE B 301 source : AC2 21) chain B residue 198 type sequence D description binding site for residue ADE B 301 source : AC2 22) chain B residue 204 type sequence Q description binding site for residue ADE B 301 source : AC2 23) chain C residue 77 type sequence A description binding site for residue ADE C 301 source : AC3 24) chain C residue 78 type sequence G description binding site for residue ADE C 301 source : AC3 25) chain C residue 151 type sequence Q description binding site for residue ADE C 301 source : AC3 26) chain C residue 152 type sequence F description binding site for residue ADE C 301 source : AC3 27) chain C residue 153 type sequence M description binding site for residue ADE C 301 source : AC3 28) chain C residue 172 type sequence V description binding site for residue ADE C 301 source : AC3 29) chain C residue 173 type sequence E description binding site for residue ADE C 301 source : AC3 30) chain C residue 174 type sequence M description binding site for residue ADE C 301 source : AC3 31) chain C residue 197 type sequence S description binding site for residue ADE C 301 source : AC3 32) chain C residue 198 type sequence D description binding site for residue ADE C 301 source : AC3 33) chain C residue 204 type sequence Q description binding site for residue ADE C 301 source : AC3 34) chain D residue 77 type sequence A description binding site for residue ADE D 301 source : AC4 35) chain D residue 78 type sequence G description binding site for residue ADE D 301 source : AC4 36) chain D residue 151 type sequence Q description binding site for residue ADE D 301 source : AC4 37) chain D residue 152 type sequence F description binding site for residue ADE D 301 source : AC4 38) chain D residue 153 type sequence M description binding site for residue ADE D 301 source : AC4 39) chain D residue 173 type sequence E description binding site for residue ADE D 301 source : AC4 40) chain D residue 174 type sequence M description binding site for residue ADE D 301 source : AC4 41) chain D residue 197 type sequence S description binding site for residue ADE D 301 source : AC4 42) chain D residue 198 type sequence D description binding site for residue ADE D 301 source : AC4 43) chain D residue 204 type sequence Q description binding site for residue ADE D 301 source : AC4 44) chain A residue 12 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 12 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI1 46) chain C residue 12 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI1 47) chain D residue 12 type ACT_SITE sequence E description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI2 49) chain B residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI2 50) chain C residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI2 51) chain D residue 198 type ACT_SITE sequence D description Proton donor => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI2 52) chain A residue 78 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 53) chain D residue 78 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 54) chain D residue 153 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 55) chain D residue 174 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 56) chain A residue 153 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 57) chain A residue 174 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 58) chain B residue 78 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 59) chain B residue 153 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 60) chain B residue 174 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 61) chain C residue 78 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 62) chain C residue 153 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3 63) chain C residue 174 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_01684 source Swiss-Prot : SWS_FT_FI3

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