eF-site ID 6fkf-ABCDEFGHIJKLMNOPQRSTabdegp PDB Code 6fkf Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, a, b, d, e, g, p Title Chloroplast F1Fo conformation 1 Classification MEMBRANE PROTEIN Compound ATP synthase subunit alpha, chloroplastic Source ORGANISM_COMMON: Spinach; ORGANISM_SCIENTIFIC: Spinacia oleracea; Sequence A:  TIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARI HGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEI TASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGR GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQK ASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYT GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPP GREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET QAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGI SVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASD LDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGT NGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTF TEEAEALLKEAIQEQMERFLLQ B:  KNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQ PMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAP LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP AFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMK ESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMA EYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG YQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP RIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEED RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRG FQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL C:  RADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHG LDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQ EGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITA SESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQ RELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKAS SVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGA ALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGR EAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQA GDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISV SRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLD KATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNG YLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTE EAEALLKEAIQEQMERFLL D:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMES E:  EISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLDE VMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEGS SVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASES RLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQREL IIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSVA QVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAALA EYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREAY PGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGDV SAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSRV GSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKAT QNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYLD SLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEAE ALLKEAIQEQMERFLLQ F:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL G:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV H:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV I:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV J:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV K:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV L:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV M:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV N:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV O:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV P:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV Q:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV R:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV S:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV T:  PLIAAASVIAAGLAVGLASIGPGVGQGTAAGQAVEGIARQ PEAEGKIRGTLLLSLAFMEALTIYGLVVALALLFANPFV a:  VGQHFYWQIGGFQIHGQVLITSWVVIAILLGSAAIAVRSP QTIPTGGQNFFEYVLEFIRDVSKTQIGEEYRPWVPFIGTM FLFIFVSNWSGALLPWKIIQLPHGELAAPTNDINTTVALA LLTSVAYFYAGLTKKGLGYFGKYIQPTPILLPINILEDFT KPLSLSFRLFGNILADELVVVVLVSLVPLVVPIPVMFLGL FTSGIQALIFATLAAAYIGESLE b:  NTDILATNLINLSVVLGVLIFFGKGVLSDLLDNRKQRILN TIRNSEELRGKAIEQLEKARARLKKVEMDADQFRVNGYSE IEREKMNLINSTYKTLEQFENYKNETIQFEQQKAINQVRQ RVFQQALQGALGTLNSCLNNELHLRTINANIGMFGAMNEI d:  VDSTASRYASALADVADVTGTLEATNSDVEKLIRIFSEEP VYYFFANPVISIDNKRSVLDEIITTSGLQPHTANFINILI DSERINLVKEILNEFEDVFNKITGTEVAVVTSVVKLENDH LAQIAKGVQKITGAKNVRIKTVIDPSLVAGFTIRYGNEGS KLVDMSVKKQLEEIAAQLE e:  MTLNLCVLTPNRSIWNSEVKEIILSTNSGQIGVLPNHAPT ATAVDIGILRIRLNDQWLTLALMGGFARIGNNEITILVND AERGSDIDPQEAQQTLEIAEANLRKAEGKRQKIEANLALR RARTRVEASNT g:  NLRELRDRIGSVKNTQKITEAMKLVAAAKVRRAQEAVVNG RPFSETLVEVLYNMNEQLQTEDVDVPLTKIRTVKKVALMV VTGDRGLCGGFNNMLLKKAESRIAELKKLGVDYTIISIGK KGNTYFIRRPEIPVDRYFDGTNLPTAKEAQAIADDVFSLF VSEEVDKVEMLYTKFVSLVKSDPVIHTLLPLSPKGEICDI NGKCVDAAEDELFRLTTKEGKLTVERDMIKTETPAFSPIL EFEQDPAQILDALLPLYLNSQILRALQESLASELAARMTA MSNATDNANELKKTLSINYNRARQAKITGEILEIVAGANA C p:  IEKASLFDFNLTLPIIMAEFLFLMFALDKIYYTPLGDFMD KRDASIKEQLSGVKDTSSEVKQLEEQANAVMRAARAEISA ALNKMKKETQLEVEAKLAEGRKKIEVELQEALGSLEQQKE DTIKSLDSQISALSDDIVKKVLP Description (1)  ATP synthase subunit alpha, chloroplastic (E.C.3.6.3.14), ATP synthase subunit beta, chloroplastic (E.C.3.6.3.14), ATP synthase delta chain, chloroplastic, ATP synthase epsilon chain, chloroplastic, ATP synthase gamma chain, chloroplastic, ATP synthase subunit a, chloroplastic, ATP synthase subunit b', chloroplastic, ATP synthase subunit b, chloroplastic, ATP synthase subunit c, chloroplastic Functional site 1) chain A residue 173 type sequence Q description binding site for residue ATP A 600 source : AC1 2) chain A residue 174 type sequence T description binding site for residue ATP A 600 source : AC1 3) chain A residue 175 type sequence G description binding site for residue ATP A 600 source : AC1 4) chain A residue 176 type sequence K description binding site for residue ATP A 600 source : AC1 5) chain A residue 177 type sequence T description binding site for residue ATP A 600 source : AC1 6) chain A residue 178 type sequence A description binding site for residue ATP A 600 source : AC1 7) chain A residue 350 type sequence F description binding site for residue ATP A 600 source : AC1 8) chain A residue 355 type sequence R description binding site for residue ATP A 600 source : AC1 9) chain A residue 423 type sequence Q description binding site for residue ATP A 600 source : AC1 10) chain A residue 425 type sequence Q description binding site for residue ATP A 600 source : AC1 11) chain F residue 376 type sequence Q description binding site for residue ATP A 600 source : AC1 12) chain A residue 177 type sequence T description binding site for residue MG A 601 source : AC2 13) chain A residue 262 type sequence D description binding site for residue MG A 601 source : AC2 14) chain B residue 378 type sequence R description binding site for residue ATP C 600 source : AC3 15) chain C residue 173 type sequence Q description binding site for residue ATP C 600 source : AC3 16) chain C residue 174 type sequence T description binding site for residue ATP C 600 source : AC3 17) chain C residue 175 type sequence G description binding site for residue ATP C 600 source : AC3 18) chain C residue 176 type sequence K description binding site for residue ATP C 600 source : AC3 19) chain C residue 177 type sequence T description binding site for residue ATP C 600 source : AC3 20) chain C residue 178 type sequence A description binding site for residue ATP C 600 source : AC3 21) chain C residue 350 type sequence F description binding site for residue ATP C 600 source : AC3 22) chain C residue 355 type sequence R description binding site for residue ATP C 600 source : AC3 23) chain C residue 423 type sequence Q description binding site for residue ATP C 600 source : AC3 24) chain C residue 425 type sequence Q description binding site for residue ATP C 600 source : AC3 25) chain C residue 177 type sequence T description binding site for residue MG C 601 source : AC4 26) chain C residue 262 type sequence D description binding site for residue MG C 601 source : AC4 27) chain D residue 173 type sequence G description binding site for residue ADP D 600 source : AC5 28) chain D residue 175 type sequence G description binding site for residue ADP D 600 source : AC5 29) chain D residue 176 type sequence V description binding site for residue ADP D 600 source : AC5 30) chain D residue 177 type sequence G description binding site for residue ADP D 600 source : AC5 31) chain D residue 178 type sequence K description binding site for residue ADP D 600 source : AC5 32) chain D residue 179 type sequence T description binding site for residue ADP D 600 source : AC5 33) chain D residue 180 type sequence V description binding site for residue ADP D 600 source : AC5 34) chain D residue 362 type sequence Y description binding site for residue ADP D 600 source : AC5 35) chain D residue 435 type sequence F description binding site for residue ADP D 600 source : AC5 36) chain D residue 438 type sequence A description binding site for residue ADP D 600 source : AC5 37) chain D residue 179 type sequence T description binding site for residue MG D 601 source : AC6 38) chain D residue 376 type sequence Q description binding site for residue ATP E 600 source : AC7 39) chain E residue 171 type sequence D description binding site for residue ATP E 600 source : AC7 40) chain E residue 172 type sequence R description binding site for residue ATP E 600 source : AC7 41) chain E residue 173 type sequence Q description binding site for residue ATP E 600 source : AC7 42) chain E residue 174 type sequence T description binding site for residue ATP E 600 source : AC7 43) chain E residue 175 type sequence G description binding site for residue ATP E 600 source : AC7 44) chain E residue 176 type sequence K description binding site for residue ATP E 600 source : AC7 45) chain E residue 177 type sequence T description binding site for residue ATP E 600 source : AC7 46) chain E residue 178 type sequence A description binding site for residue ATP E 600 source : AC7 47) chain E residue 350 type sequence F description binding site for residue ATP E 600 source : AC7 48) chain E residue 355 type sequence R description binding site for residue ATP E 600 source : AC7 49) chain E residue 356 type sequence P description binding site for residue ATP E 600 source : AC7 50) chain E residue 423 type sequence Q description binding site for residue ATP E 600 source : AC7 51) chain E residue 425 type sequence Q description binding site for residue ATP E 600 source : AC7 52) chain E residue 177 type sequence T description binding site for residue MG E 601 source : AC8 53) chain E residue 365 type sequence S description binding site for residue ADP F 600 source : AC9 54) chain E residue 366 type sequence R description binding site for residue ADP F 600 source : AC9 55) chain F residue 173 type sequence G description binding site for residue ADP F 600 source : AC9 56) chain F residue 175 type sequence G description binding site for residue ADP F 600 source : AC9 57) chain F residue 177 type sequence G description binding site for residue ADP F 600 source : AC9 58) chain F residue 178 type sequence K description binding site for residue ADP F 600 source : AC9 59) chain F residue 179 type sequence T description binding site for residue ADP F 600 source : AC9 60) chain F residue 180 type sequence V description binding site for residue ADP F 600 source : AC9 61) chain F residue 362 type sequence Y description binding site for residue ADP F 600 source : AC9 62) chain F residue 435 type sequence F description binding site for residue ADP F 600 source : AC9 63) chain F residue 438 type sequence A description binding site for residue ADP F 600 source : AC9 64) chain F residue 441 type sequence F description binding site for residue ADP F 600 source : AC9 65) chain F residue 442 type sequence T description binding site for residue ADP F 600 source : AC9 66) chain F residue 179 type sequence T description binding site for residue MG F 601 source : AD1 67) chain F residue 204 type sequence E description binding site for residue MG F 601 source : AD1 68) chain S residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 69) chain Q residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 70) chain R residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 71) chain R residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 72) chain M residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 73) chain M residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 74) chain T residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 75) chain T residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 76) chain G residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 77) chain G residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 78) chain H residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 79) chain S residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 80) chain H residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 81) chain L residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 82) chain L residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 83) chain K residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 84) chain K residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 85) chain J residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 86) chain J residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 87) chain I residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 88) chain I residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 89) chain N residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 90) chain N residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 91) chain O residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 92) chain O residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 93) chain P residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 94) chain P residue 57-77 type TRANSMEM sequence LAFMEALTIYGLVVALALLFA description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 95) chain Q residue 3-23 type TRANSMEM sequence PLIAAASVIAAGLAVGLASIG description Helical => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI1 96) chain S residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 97) chain H residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 98) chain L residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 99) chain K residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 100) chain J residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 101) chain I residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 102) chain N residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 103) chain O residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 104) chain P residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 105) chain Q residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 106) chain R residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 107) chain M residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 108) chain T residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 109) chain G residue 61 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396 source Swiss-Prot : SWS_FT_FI2 110) chain a residue 185-194 type prosite sequence SLSFRLFGNI description ATPASE_A ATP synthase a subunit signature. SLSFRLFGNI source prosite : PS00449 111) chain d residue 207-226 type prosite sequence VRIKTVIDPSLVAGFTIRYG description ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. VrIktvIDpSLvAGFTIRyG source prosite : PS00389 112) chain S residue 40-61 type prosite sequence ARQPEAEGKIRGTLLLSLAFME description ATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE source prosite : PS00605 113) chain g residue 349-362 type prosite sequence ITGEILEIVAGANA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITgEilEivaGAnA source prosite : PS00153 114) chain B residue 363-372 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 115) chain A residue 356-365 type prosite sequence PAINVGISVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152

Display surface Download Links