eF-site ID 1h8h-ABCDEFG PDB Code 1h8h Chain A, B, C, D, E, F, G click to enlarge Title Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP Classification HYDROLASE Compound BOVINE MITOCHONDRIAL F1-ATPASE Source ORGANISM_COMMON: CATTLE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTN FLAGFEA B:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQG QYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSH VISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA C:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP SKITKFENAFLSHVISQHQALLGKIRTDGKISEESDAKLK EIVTNFLAGFEA D:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLAE E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA F:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA G:  ATLKDITRRLKSIKNIQKITKSMKMVAAAKYARAERELKP ARVYLCGAIHSSVAKQMKLANIIYYSLKESTTSEQSARMT AMDNASKNASEMIDKLTLTFNRTRQAVITKELIEIISGAA AL Description Functional site 1) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 601 source : AC1 2) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE MG B 601 source : AC2 3) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 601 source : AC3 4) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE MG D 601 source : AC4 5) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 E 602 source : AC5 6) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 E 602 source : AC5 7) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 E 602 source : AC5 8) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : AC6 9) chain F residue 192 type sequence E description BINDING SITE FOR RESIDUE MG F 601 source : AC6 10) chain A residue 171 type sequence R description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 11) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 12) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 13) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 14) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 15) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 16) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 17) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 18) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 19) chain A residue 363 type sequence P description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 20) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 21) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC7 22) chain B residue 171 type sequence R description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 23) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 24) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 25) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 26) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 27) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 28) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 29) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 30) chain B residue 430 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 31) chain B residue 431 type sequence G description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 32) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 33) chain E residue 359 type sequence D description BINDING SITE FOR RESIDUE ATP B 600 source : AC8 34) chain C residue 171 type sequence R description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 35) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 36) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 37) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 38) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 39) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 40) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 41) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 42) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 43) chain C residue 363 type sequence P description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 44) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 45) chain C residue 431 type sequence G description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 46) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC9 47) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 48) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 49) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 50) chain D residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 51) chain D residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 52) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 53) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 54) chain D residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 55) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 56) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 57) chain D residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 58) chain D residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 59) chain D residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : BC1 60) chain B residue 343 type sequence I description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 61) chain B residue 344 type sequence S description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 62) chain B residue 371 type sequence V description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 63) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 64) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 65) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 66) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 67) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 68) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 69) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 70) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 71) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 72) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 73) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 74) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 75) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 76) chain F residue 425 type sequence T description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 77) chain B residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL B 701 source : BC3 78) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL B 701 source : BC3 79) chain B residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL B 701 source : BC3 80) chain B residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL B 701 source : BC3 81) chain B residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL B 701 source : BC3 82) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 83) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 84) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 85) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 86) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 87) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 88) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 89) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 90) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 91) chain G residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 92) chain E residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 93) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 94) chain B residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 95) chain C residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 96) chain C residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 97) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 98) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 99) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 100) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 101) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 102) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 103) chain G residue 24 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 104) chain G residue 245 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 105) chain F residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 106) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 107) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 108) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 109) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 110) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 111) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 112) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 113) chain D residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 114) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 115) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 116) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 117) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 118) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 119) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 120) chain G residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 121) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 122) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 123) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 124) chain E residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 125) chain E residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 126) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 127) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 128) chain B residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 129) chain B residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 130) chain E residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 131) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 132) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 133) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 134) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 135) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 136) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 137) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 138) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 139) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 140) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 141) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 142) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 143) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 144) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 145) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 146) chain B residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 147) chain B residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 148) chain B residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 149) chain B residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 150) chain D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 151) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 152) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 153) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 154) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 155) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 156) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 157) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 158) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 159) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 160) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 161) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 162) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 163) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 164) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 165) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 166) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 167) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 168) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 169) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 170) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 171) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 172) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 173) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 174) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 175) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 176) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 177) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 178) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 179) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 180) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 181) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 182) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 183) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 184) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 185) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 186) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 187) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 188) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 189) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 190) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 191) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 192) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 193) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152 194) 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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