eF-site ID 1bmf-ABCDEFG PDB Code 1bmf Chain A, B, C, D, E, F, G click to enlarge Title BOVINE MITOCHONDRIAL F1-ATPASE Classification ATP PHOSPHORYLASE 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 KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTN FLAGFEA 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 175 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 2) chain B residue 175 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 3) chain C residue 175 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 4) chain D residue 162 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 5) chain E residue 162 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 6) chain F residue 162 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 7) chain D residue 188 type sequence E description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 8) chain C residue 373 type sequence R description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 9) chain E residue 188 type sequence E description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 10) chain A residue 373 type sequence R description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 11) chain F residue 188 type sequence E description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 12) chain B residue 373 type sequence R description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 13) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 601 source : AC1 14) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE MG B 601 source : AC2 15) chain B residue 269 type sequence D description BINDING SITE FOR RESIDUE MG B 601 source : AC2 16) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 601 source : AC3 17) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE MG D 601 source : AC4 18) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : AC5 19) chain F residue 188 type sequence E description BINDING SITE FOR RESIDUE MG F 601 source : AC5 20) chain A residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 21) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 22) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 23) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 24) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 25) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 26) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 27) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 28) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 29) chain A residue 363 type sequence P description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 30) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 31) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 32) chain B residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 33) chain B residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 34) chain B residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 35) chain B residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 36) chain B residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 37) chain B residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 38) chain B residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 39) chain B residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 40) chain B residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 41) chain B residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 42) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP B 600 source : AC7 43) chain C residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 44) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 45) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 46) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 47) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 48) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 49) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 50) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 51) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 52) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 53) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 54) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 55) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 56) chain D residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 57) chain D residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 58) chain D residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 59) chain D residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 60) chain D residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 61) chain D residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 62) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 63) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 64) chain D residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 65) chain D residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 66) chain B residue 344 type sequence S description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 67) chain B residue 371 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 68) chain B residue 373 type sequence R description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 69) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 70) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 71) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 72) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 73) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 74) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 75) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 76) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 77) chain F residue 311 type sequence Y description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 78) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 79) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 80) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 81) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 82) chain G residue 14 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 83) chain E residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 84) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 86) chain C residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 87) chain C residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 88) chain G residue 24 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 89) chain G residue 245 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 90) chain F residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 91) chain D residue 162 type catalytic sequence K description 178 source MCSA : MCSA1 92) chain D residue 188 type catalytic sequence E description 178 source MCSA : MCSA1 93) chain D residue 189 type catalytic sequence R description 178 source MCSA : MCSA1 94) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 95) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 96) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 97) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 98) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 99) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 100) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 101) chain B residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 102) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 103) chain G residue 30 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 104) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 105) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 106) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 107) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 108) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 109) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 110) chain D residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 111) chain D residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 112) chain D residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 113) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 114) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 115) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 116) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 117) chain G residue 90 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 118) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 119) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 120) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 121) chain E residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 122) chain E residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 123) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 124) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 125) chain B residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 126) chain B residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 127) chain G residue 258-271 type prosite sequence ITKELIEIISGAAA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA source prosite : PS00153 128) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 129) chain B residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 130) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 131) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 132) chain B residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 133) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 134) chain E residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 135) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 136) chain D residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 137) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 138) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 139) chain D residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 140) chain B residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 141) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 142) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 143) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 144) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 145) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 146) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 147) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 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 D residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 155) chain D residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 156) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 157) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 158) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 159) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 160) chain D residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 161) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 162) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 163) chain B residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 164) chain B residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 165) chain B residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 166) chain B residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 167) chain B residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 168) chain B residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 169) chain B residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 170) chain B residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 171) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 172) chain B residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 173) chain B residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 174) chain B residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 175) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 176) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 177) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 178) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 179) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 180) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 181) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 182) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 183) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 184) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 185) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 186) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 187) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 188) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 189) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 190) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 191) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 192) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 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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