eF-site ID 1h8e-ABCDEFGHI PDB Code 1h8e Chain A, B, C, D, E, F, G, H, I click to enlarge Title (ADP.AlF4)2(ADP.SO4) bovine F1-ATPase (all three catalytic sites occupied) Classification HYDROLASE Compound BOVINE MITOCHONDRIAL F1-ATPASE Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA QTRAMKQVAGTMKLELAQYREVAAFLDAATQQLLSRGVRL TELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKF ENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTNF LAGFEA B:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQG QYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSH VISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA C:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA QTRAMKQVAGTMKLELAQYREVAAFADLDAATQQLLSRGV RLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKIT KFENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVT NFLAGFEA D:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLAE E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMEQ EILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELI NNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKD ATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQD VLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMG TMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLD ATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDV ARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKI QRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGEYD HLPEQAFYMVGPIE F:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA G:  ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKP ARVYGVGSLALYEKADILIIGVSSDRGLCGAIHSSVAKQM KSEAANLKEVKIIGVGDKIRSILHTFKEVGRRPPTFGDAS VIALELLNEGSIIFNRFRSVISYKTEEKPIFSLDTISSAE SMSIYDDIDADVLRNYQEYSLANIIYYSLKESTTSEQSAR MTAMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISG AAAL H:  QMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPT LQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLA EEAVTLDML I:  VAYWRQAGLSYIRYSQICAKAVRDATSGSTIKIVKV Description Functional site 1) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 2) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 3) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 4) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 5) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 6) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 7) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 8) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 9) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 10) chain D residue 368 type sequence Y description BINDING SITE FOR RESIDUE ADP A 600 source : AC1 11) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 601 source : AC2 12) chain A residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL A 602 source : AC3 13) chain A residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL A 602 source : AC3 14) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL A 602 source : AC3 15) chain A residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL A 602 source : AC3 16) chain B residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL B 602 source : AC4 17) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL B 602 source : AC4 18) chain B residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL B 602 source : AC4 19) chain B residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL B 602 source : AC4 20) chain B residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL B 602 source : AC4 21) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 22) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 23) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 24) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 25) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 26) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 27) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 28) chain B residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 29) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP B 600 source : AC5 30) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE MG B 601 source : AC6 31) chain B residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL B 602 source : AC7 32) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL B 602 source : AC7 33) chain B residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL B 602 source : AC7 34) chain B residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL B 602 source : AC7 35) chain B residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL B 602 source : AC7 36) chain B residue 349 type sequence Q description BINDING SITE FOR RESIDUE GOL B 700 source : AC8 37) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE GOL B 700 source : AC8 38) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE GOL B 700 source : AC8 39) chain F residue 337 type sequence R description BINDING SITE FOR RESIDUE GOL B 700 source : AC8 40) chain F residue 341 type sequence E description BINDING SITE FOR RESIDUE GOL B 700 source : AC8 41) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 42) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 43) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 44) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 45) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 46) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 47) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 48) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 49) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 50) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP C 600 source : AC9 51) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 601 source : BC1 52) chain C residue 62 type sequence M description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 53) chain C residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 54) chain C residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 55) chain C residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 56) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 57) chain C residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL C 602 source : BC2 58) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 59) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 60) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 61) chain D residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 62) chain D residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 63) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 64) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 65) chain D residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 66) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 67) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 68) chain D residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 69) chain D residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 70) chain D residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : BC3 71) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE MG D 601 source : BC4 72) chain C residue 344 type sequence S description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 73) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 74) chain D residue 158 type sequence A description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 75) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 76) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 77) chain D residue 188 type sequence E description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 78) chain D residue 189 type sequence R description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 79) chain D residue 311 type sequence Y description BINDING SITE FOR RESIDUE ALF D 620 source : BC5 80) chain A residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 81) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 82) chain E residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 83) chain E residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 84) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 85) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 86) chain E residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 87) chain E residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 88) chain E residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP E 600 source : BC6 89) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE MG E 601 source : BC7 90) chain A residue 373 type sequence R description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 91) chain E residue 158 type sequence A description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 92) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 93) chain E residue 189 type sequence R description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 94) chain E residue 260 type sequence R description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 95) chain E residue 311 type sequence Y description BINDING SITE FOR RESIDUE SO4 E 630 source : BC8 96) chain B residue 371 type sequence V description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 97) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 98) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 99) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 100) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 101) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 102) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 103) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 104) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 105) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 106) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 107) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP F 600 source : BC9 108) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : CC1 109) chain B residue 344 type sequence S description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 110) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 111) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 112) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 113) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 114) chain F residue 188 type sequence E description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 115) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 116) chain F residue 311 type sequence Y description BINDING SITE FOR RESIDUE ALF F 620 source : CC2 117) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 118) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 119) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 120) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 121) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 122) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 123) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 124) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 125) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 126) chain I residue 21 type MOD_RES sequence A description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 127) chain I residue 37 type MOD_RES sequence T description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 128) chain B residue 430 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 129) chain C residue 170 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 130) chain C residue 430 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 131) chain I residue 44 type MOD_RES sequence I description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 132) chain G residue 245 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 133) chain F residue 189 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 134) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 135) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 136) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 137) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 138) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 139) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 140) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 141) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 142) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 143) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 144) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 145) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 146) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 147) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 148) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 149) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 150) chain G residue 172 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 151) chain D residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 152) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 153) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 154) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 155) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 156) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 157) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 158) chain G residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 159) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 160) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 161) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 162) chain G residue 129 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 163) chain E residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 164) chain E residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 165) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 166) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 167) chain B residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 168) chain B residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 169) chain E residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 170) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 171) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 172) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 173) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 174) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 175) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 176) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 177) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 178) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 179) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 180) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 181) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 182) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 183) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 184) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 185) chain B residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 186) chain B residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 187) chain B residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 188) chain B residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 189) chain D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 190) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 191) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 192) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 193) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 194) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 195) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 196) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 197) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 198) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 199) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 200) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 201) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 202) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 203) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 204) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 205) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 206) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 207) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 208) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 209) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 210) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 211) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 212) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 213) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 214) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 215) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 216) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 217) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 218) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 219) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 220) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 221) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 222) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 223) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 224) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 225) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 226) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 227) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 228) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152 229) chain D residue 346-355 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152

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