eF-site ID 1w0j-ABCDEFG PDB Code 1w0j Chain A, B, C, D, E, F, G click to enlarge Title Beryllium fluoride inhibited bovine F1-ATPase Classification HYDROLASE Compound ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, MITOCHONDRIAL PRECURSOR Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTN FLAGFEA B:  VDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGM SLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEE LLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISV REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDT IINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTD ADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH SRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNV ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRA MKQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQ GQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLS HVISQHQALLGKIRTDGKISEESDAKLKEIVTNFLAGFEA C:  EERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEM VEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTG AIVDVPVGEELLGRVVDALGNAIDGKGPIGSKARRRVGLK APGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQ TGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRST VAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCS MGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGRE AYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAG DVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVS RVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDA ATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGY LDKLEPSKITKFENAFLSHVISQHQALLGKIRTDGKISEE SDAKLKEIVTNFLAGFEA 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 ARVYGVGLIIGVSSDRGLCGAIHSSVAKQMKIIGVGDKIR SILTFKEVGRRPPTFGDASVIALELSIIFNRFRSVISYKT LRNYQEYSLANIIYYSLKESTTSEQSARMTAMDNASKNAS EMIDKLTLTFNRTRQAVITKELIEIISGAAAL Description Functional site 1) chain E residue 158 type sequence A description BINDING SITE FOR RESIDUE PO4 E 1475 source : AC1 2) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : AC1 3) chain E residue 161 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : AC1 4) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 E 1475 source : AC1 5) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 E 1475 source : AC1 6) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 1512 source : AC2 7) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE MG B 1512 source : AC3 8) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 1512 source : AC4 9) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE MG D 1477 source : AC5 10) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 1476 source : AC6 11) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 12) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 13) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 14) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 15) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 16) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 17) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 18) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 19) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 20) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 21) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 22) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 23) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 24) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 25) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 26) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 27) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 28) chain B residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 29) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 30) chain E residue 356 type sequence R description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 31) chain E residue 359 type sequence D description BINDING SITE FOR RESIDUE ADP B 1511 source : AC8 32) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 33) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 34) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 35) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 36) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 37) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 38) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 39) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 40) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 41) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 42) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 43) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 44) chain D residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 45) chain D residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 46) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 47) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 48) chain D residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 49) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 50) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 51) chain D residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 52) chain D residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 53) chain D residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 54) chain C residue 344 type sequence S description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 55) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 56) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 57) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 58) chain D residue 188 type sequence E description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 59) chain D residue 189 type sequence R description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 60) chain D residue 311 type sequence Y description BINDING SITE FOR RESIDUE BEF D 1478 source : BC2 61) chain B residue 371 type sequence V description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 62) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 63) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 64) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 65) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 66) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 67) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 68) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 69) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 70) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 71) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 72) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 73) chain F residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP F 1475 source : BC3 74) chain B residue 343 type sequence I description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 75) chain B residue 344 type sequence S description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 76) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 77) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 78) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 79) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 80) chain F residue 188 type sequence E description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 81) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE BEF F 1477 source : BC4 82) chain A residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 83) chain A residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 84) chain A residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 85) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 86) chain A residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 87) chain B residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL B 1513 source : BC6 88) chain B residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1513 source : BC6 89) chain B residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL B 1513 source : BC6 90) chain B residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL B 1513 source : BC6 91) chain C residue 62 type sequence M description BINDING SITE FOR RESIDUE GOL C 1513 source : BC7 92) chain C residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL C 1513 source : BC7 93) chain C residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC7 94) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC7 95) chain C residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL C 1513 source : BC7 96) chain D residue 231 type sequence R description BINDING SITE FOR RESIDUE GOL D 1475 source : BC8 97) chain D residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL D 1475 source : BC8 98) chain D residue 274 type sequence R description BINDING SITE FOR RESIDUE GOL D 1475 source : BC8 99) chain D residue 288 type sequence D description BINDING SITE FOR RESIDUE GOL D 1475 source : BC8 100) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 101) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 102) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 103) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 104) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 105) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 106) chain D residue 346-355 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 107) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 108) chain E residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 109) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 110) chain B residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 111) chain C residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 112) chain C residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 113) chain G residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 114) chain G residue 245 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 115) chain F residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 116) chain G residue 24 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 117) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 118) chain G residue 172 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 119) chain D residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 120) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 121) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 122) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 123) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 124) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 125) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 126) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 127) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 128) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 129) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 130) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 131) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 132) chain G residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 133) chain G residue 129 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 134) chain E residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 135) chain E residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 136) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 137) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 138) chain B residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 139) chain B residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 140) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 141) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 142) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 143) chain E residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 144) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 145) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 146) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 147) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 148) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 149) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 150) chain B residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 151) chain B residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 152) chain B residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 153) chain B residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 154) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 155) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 156) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 157) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 158) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 159) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 160) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 161) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 162) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 163) chain D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 164) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 165) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 166) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 167) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 168) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 169) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 170) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 171) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 172) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 173) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 174) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 175) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 176) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 177) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 178) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 179) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 180) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 181) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 182) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 183) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 184) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 185) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 186) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 187) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 188) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 189) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 190) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 191) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 192) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 193) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 194) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 195) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 196) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 197) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 198) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 199) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 200) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 201) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 202) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 203) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 204) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 205) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 206) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 207) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 208) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 209) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 210) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 211) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 212) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 213) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 214) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3

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