eF-site ID 2w6i-ABCDEFGHI PDB Code 2w6i Chain A, B, C, D, E, F, G, H, I click to enlarge Title Low resolution structures of bovine mitochondrial F1-ATPase during controlled dehydration: Hydration State 4B. Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM, MITOCHONDRIAL Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTN FLAGFEA B:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQG QYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSH VISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFEA C:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP SKITKFENAFLSHVISQHQALLSKIRTDGKISEESDAKLK 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 ARVYGVGSLALYEKADIKTPELIIGVSSDRGLCGAIHSSV AKQMKSEAANLKEVKIIGVGDKIRSILHRTHSDQFLVTFK EVGRRPPTFGDASVIALELLNSGYEFDEGSIIFNRFRSVI SYKTEEKPIFSLDTISSAESMSIYDDIDADVLRNYQEYSL ANIIYYSLKESTTSEQSARMTAMDNASKNASEMIDKLTLT FNRTRQAVITKELIEIISGAAAL H:  FTFASTQVSGSVTVNSVQLLAEEIQIRIEAN I:  RQAGLSYIRYSQICAKAVSGSTIKIVKV Description Functional site 1) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 2) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 3) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 4) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 5) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 6) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 7) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 8) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 9) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 10) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 11) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 12) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 13) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 14) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 15) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 16) chain G residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 17) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 18) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 19) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 20) chain G residue 129 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 21) chain E residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 22) chain E residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 23) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 24) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 25) chain B residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 27) chain G residue 121 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 28) chain E residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 29) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 30) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 31) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 32) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 33) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 34) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 35) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 36) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 37) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 38) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 39) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 40) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 41) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 42) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 43) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 44) chain B residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 45) chain B residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 46) chain B residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 47) chain B residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 48) chain D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 49) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 50) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 51) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 52) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 53) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 54) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 55) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 56) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 57) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 58) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 59) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 60) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 61) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 62) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 63) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 64) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 65) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 66) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 67) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 68) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 69) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 70) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 71) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 72) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 73) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 74) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 75) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 76) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 77) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 78) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 79) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 80) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 81) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 82) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 83) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 84) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 85) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 86) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 87) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 88) chain I residue 20 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 89) chain B residue 430 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 90) chain C residue 170 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 91) chain C residue 430 type MOD_RES sequence Q description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI1 92) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 93) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 94) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 95) chain I residue 43 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 96) chain G residue 245 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 97) chain F residue 189 type MOD_RES sequence R description N6-acetyllysine => ECO:0000250|UniProtKB:P56382 source Swiss-Prot : SWS_FT_FI2 98) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 99) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 100) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 101) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 102) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 103) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 104) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 105) chain G residue 172 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 106) chain D residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 107) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 108) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 109) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 110) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 111) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 112) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 113) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152 114) 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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