eF-site ID 6fki-ABCDEFGHIJKLMNOPQRSTabdegp PDB Code 6fki 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 3 Classification MEMBRANE PROTEIN Compound ATP synthase subunit a, chloroplastic Source ORGANISM_COMMON: Spinach; ORGANISM_SCIENTIFIC: Spinacia oleracea; Sequence A:  TIRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARI HGLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLM IQEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEI TASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGR GQRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQK ASSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYT GAALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPP GREAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVET QAGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGI SVSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASD LDKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGT NGYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTF TEEAEALLKEAIQEQMERFLL B:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMES C:  IRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIH GLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIT ASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRG QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKA SSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTG AALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPG REAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQ AGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGIS VSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDL DKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTN GYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFT EEAEALLKEAIQEQMERFLLQ D:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL E:  DEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLD EVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASE SRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRE LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSV AQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAAL AEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREA YPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGD VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR VGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKA TQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYL DSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEA EALLKEAIQEQMERFLLQ F:  KNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQ PMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAP LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP AFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMK ESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMA EYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG YQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP RIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEED RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRG FQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL 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:  FNTDILATNLINLSVVLGVLIFFGKGVLSDLLDNRKQRIL NTIRNSEELRGKAIEQLEKARARLKKVEMDADQFRVNGYS EIEREKMNLINSTYKTLEQFENYKNETIQFEQQKAINQVR QRVFQQALQGALGTLNSCLNNELHLRTINANIGMFGAMNE I 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 a, chloroplastic, ATP synthase subunit b, chloroplastic, ATP synthase delta chain, chloroplastic, ATP synthase subunit b', chloroplastic, ATP synthase epsilon chain, chloroplastic, ATP synthase gamma chain, chloroplastic, ATP synthase subunit c, chloroplastic, ATP synthase subunit alpha, chloroplastic (E.C.3.6.3.14), ATP synthase subunit beta, chloroplastic (E.C.3.6.3.14) Functional site 1) chain D residue 376 type sequence Q description binding site for residue ATP E 600 source : AC1 2) chain E residue 173 type sequence Q description binding site for residue ATP E 600 source : AC1 3) chain E residue 174 type sequence T description binding site for residue ATP E 600 source : AC1 4) chain E residue 175 type sequence G description binding site for residue ATP E 600 source : AC1 5) chain E residue 176 type sequence K description binding site for residue ATP E 600 source : AC1 6) chain E residue 177 type sequence T description binding site for residue ATP E 600 source : AC1 7) chain E residue 178 type sequence A description binding site for residue ATP E 600 source : AC1 8) chain E residue 350 type sequence F description binding site for residue ATP E 600 source : AC1 9) chain E residue 355 type sequence R description binding site for residue ATP E 600 source : AC1 10) chain E residue 423 type sequence Q description binding site for residue ATP E 600 source : AC1 11) chain E residue 425 type sequence Q description binding site for residue ATP E 600 source : AC1 12) chain E residue 177 type sequence T description binding site for residue MG E 601 source : AC2 13) chain A residue 173 type sequence Q description binding site for residue ATP A 600 source : AC3 14) chain A residue 174 type sequence T description binding site for residue ATP A 600 source : AC3 15) chain A residue 175 type sequence G description binding site for residue ATP A 600 source : AC3 16) chain A residue 176 type sequence K description binding site for residue ATP A 600 source : AC3 17) chain A residue 177 type sequence T description binding site for residue ATP A 600 source : AC3 18) chain A residue 178 type sequence A description binding site for residue ATP A 600 source : AC3 19) chain A residue 350 type sequence F description binding site for residue ATP A 600 source : AC3 20) chain A residue 355 type sequence R description binding site for residue ATP A 600 source : AC3 21) chain A residue 423 type sequence Q description binding site for residue ATP A 600 source : AC3 22) chain A residue 425 type sequence Q description binding site for residue ATP A 600 source : AC3 23) chain F residue 378 type sequence R description binding site for residue ATP A 600 source : AC3 24) chain A residue 177 type sequence T description binding site for residue MG A 601 source : AC4 25) chain A residue 201 type sequence Q description binding site for residue MG A 601 source : AC4 26) chain A residue 366 type sequence R description binding site for residue ADP B 501 source : AC5 27) chain B residue 173 type sequence G description binding site for residue ADP B 501 source : AC5 28) chain B residue 175 type sequence G description binding site for residue ADP B 501 source : AC5 29) chain B residue 177 type sequence G description binding site for residue ADP B 501 source : AC5 30) chain B residue 178 type sequence K description binding site for residue ADP B 501 source : AC5 31) chain B residue 179 type sequence T description binding site for residue ADP B 501 source : AC5 32) chain B residue 180 type sequence V description binding site for residue ADP B 501 source : AC5 33) chain B residue 205 type sequence R description binding site for residue ADP B 501 source : AC5 34) chain B residue 362 type sequence Y description binding site for residue ADP B 501 source : AC5 35) chain B residue 435 type sequence F description binding site for residue ADP B 501 source : AC5 36) chain B residue 438 type sequence A description binding site for residue ADP B 501 source : AC5 37) chain B residue 441 type sequence F description binding site for residue ADP B 501 source : AC5 38) chain B residue 179 type sequence T description binding site for residue MG B 502 source : AC6 39) chain B residue 205 type sequence R description binding site for residue MG B 502 source : AC6 40) chain B residue 376 type sequence Q description binding site for residue ATP C 601 source : AC7 41) chain C residue 172 type sequence R description binding site for residue ATP C 601 source : AC7 42) chain C residue 173 type sequence Q description binding site for residue ATP C 601 source : AC7 43) chain C residue 174 type sequence T description binding site for residue ATP C 601 source : AC7 44) chain C residue 175 type sequence G description binding site for residue ATP C 601 source : AC7 45) chain C residue 176 type sequence K description binding site for residue ATP C 601 source : AC7 46) chain C residue 177 type sequence T description binding site for residue ATP C 601 source : AC7 47) chain C residue 178 type sequence A description binding site for residue ATP C 601 source : AC7 48) chain C residue 321 type sequence E description binding site for residue ATP C 601 source : AC7 49) chain C residue 350 type sequence F description binding site for residue ATP C 601 source : AC7 50) chain C residue 355 type sequence R description binding site for residue ATP C 601 source : AC7 51) chain C residue 356 type sequence P description binding site for residue ATP C 601 source : AC7 52) chain C residue 423 type sequence Q description binding site for residue ATP C 601 source : AC7 53) chain C residue 425 type sequence Q description binding site for residue ATP C 601 source : AC7 54) chain C residue 177 type sequence T description binding site for residue MG C 602 source : AC8 55) chain C residue 364 type sequence V description binding site for residue ADP D 600 source : AC9 56) chain C residue 365 type sequence S description binding site for residue ADP D 600 source : AC9 57) chain C residue 366 type sequence R description binding site for residue ADP D 600 source : AC9 58) chain D residue 173 type sequence G description binding site for residue ADP D 600 source : AC9 59) chain D residue 175 type sequence G description binding site for residue ADP D 600 source : AC9 60) chain D residue 176 type sequence V description binding site for residue ADP D 600 source : AC9 61) chain D residue 177 type sequence G description binding site for residue ADP D 600 source : AC9 62) chain D residue 178 type sequence K description binding site for residue ADP D 600 source : AC9 63) chain D residue 179 type sequence T description binding site for residue ADP D 600 source : AC9 64) chain D residue 180 type sequence V description binding site for residue ADP D 600 source : AC9 65) chain D residue 362 type sequence Y description binding site for residue ADP D 600 source : AC9 66) chain D residue 435 type sequence F description binding site for residue ADP D 600 source : AC9 67) chain D residue 438 type sequence A description binding site for residue ADP D 600 source : AC9 68) chain D residue 441 type sequence F description binding site for residue ADP D 600 source : AC9 69) chain D residue 442 type sequence T description binding site for residue ADP D 600 source : AC9 70) chain D residue 179 type sequence T description binding site for residue MG D 601 source : AD1 71) chain D residue 204 type sequence E description binding site for residue MG D 601 source : AD1 72) chain A residue 9 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 73) chain A residue 10 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 74) chain A residue 11 type sequence K description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 75) chain A residue 14 type sequence R description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 76) chain p residue 203 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 77) chain p residue 204 type sequence D description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 78) chain p residue 205 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 79) chain p residue 207 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 80) chain p residue 208 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 81) chain p residue 209 type sequence A description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 82) chain p residue 210 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD2 83) chain A residue 9 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 84) chain A residue 10 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 85) chain A residue 11 type sequence K description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 86) chain A residue 14 type sequence R description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 87) chain p residue 203 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 88) chain p residue 204 type sequence D description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 89) chain p residue 205 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 90) chain p residue 207 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 91) chain p residue 208 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 92) chain p residue 209 type sequence A description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 93) chain p residue 210 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD3 94) chain A residue 9 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 95) chain A residue 10 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 96) chain A residue 11 type sequence K description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 97) chain A residue 14 type sequence R description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 98) chain p residue 203 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 99) chain p residue 204 type sequence D description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 100) chain p residue 205 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 101) chain p residue 207 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 102) chain p residue 208 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 103) chain p residue 209 type sequence A description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 104) chain p residue 210 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD4 105) chain A residue 9 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 106) chain A residue 10 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 107) chain A residue 11 type sequence K description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 108) chain A residue 14 type sequence R description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 109) chain p residue 203 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 110) chain p residue 204 type sequence D description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 111) chain p residue 205 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 112) chain p residue 207 type sequence I description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 113) chain p residue 208 type sequence S description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 114) chain p residue 209 type sequence A description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 115) chain p residue 210 type sequence L description binding site for Ligand GLN p 206 bound to SER A 10 source : AD5 116) chain A residue 69 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD6 117) chain A residue 70 type sequence N description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD6 118) chain d residue 72 type sequence D description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD6 119) chain d residue 76 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD6 120) chain d residue 164 type sequence E description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD6 121) chain A residue 69 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD7 122) chain A residue 70 type sequence N description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD7 123) chain d residue 72 type sequence D description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD7 124) chain d residue 76 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD7 125) chain d residue 164 type sequence E description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD7 126) chain A residue 69 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD8 127) chain A residue 70 type sequence N description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD8 128) chain d residue 72 type sequence D description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD8 129) chain d residue 76 type sequence S description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD8 130) chain d residue 164 type sequence E description binding site for Ligand VAL d 71 bound to ASN A 70 source : AD8 131) chain A residue 283 type sequence G description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 132) chain A residue 285 type sequence E description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 133) chain A residue 286 type sequence A description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 134) chain A residue 287 type sequence Y description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 135) chain A residue 289 type sequence G description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 136) chain A residue 293 type sequence Y description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 137) chain A residue 327 type sequence V description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 138) chain A residue 332 type sequence P description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 139) chain A residue 334 type sequence N description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 140) chain A residue 335 type sequence V description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 141) chain A residue 337 type sequence S description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 142) chain A residue 338 type sequence I description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 143) chain A residue 339 type sequence T description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 144) chain B residue 205 type sequence R description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 145) chain B residue 243 type sequence P description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 146) chain B residue 246 type sequence R description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 147) chain B residue 280 type sequence Q description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 148) chain B residue 281 type sequence A description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 149) chain B residue 282 type sequence G description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 150) chain B residue 283 type sequence S description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 151) chain B residue 285 type sequence V description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 152) chain B residue 286 type sequence S description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 153) chain B residue 287 type sequence A description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 154) chain B residue 288 type sequence L description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 155) chain B residue 296 type sequence V description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 156) chain B residue 298 type sequence Y description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 157) chain B residue 330 type sequence P description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 158) chain B residue 333 type sequence D description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 159) chain B residue 334 type sequence L description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 160) chain B residue 335 type sequence T description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 161) chain B residue 337 type sequence P description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 162) chain B residue 338 type sequence A description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 163) chain B residue 339 type sequence P description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 164) chain B residue 340 type sequence A description binding site for Di-peptide ARG A 284 and ASP B 336 source : AD9 165) chain C residue 5 type sequence R description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 166) chain C residue 6 type sequence A description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 167) chain C residue 8 type sequence E description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 168) chain C residue 9 type sequence I description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 169) chain C residue 12 type sequence I description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 170) chain C residue 33 type sequence L description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 171) chain C residue 68 type sequence E description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 172) chain C residue 69 type sequence S description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 173) chain C residue 71 type sequence N description binding site for Di-peptide ASP C 7 and ASN C 70 source : AE1 174) chain C residue 110 type sequence N description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 175) chain C residue 112 type sequence L description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 176) chain C residue 113 type sequence A description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 177) chain C residue 198 type sequence A description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 178) chain C residue 199 type sequence I description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 179) chain C residue 200 type sequence G description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 180) chain C residue 201 type sequence Q description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 181) chain C residue 226 type sequence A description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 182) chain C residue 228 type sequence T description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 183) chain C residue 231 type sequence S description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 184) chain C residue 235 type sequence L description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 185) chain C residue 239 type sequence A description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 186) chain C residue 242 type sequence T description binding site for Di-peptide ALA C 111 and GLU C 227 source : AE2 187) chain F residue 172 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 188) chain Q residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 189) chain R residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 190) chain R residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 191) chain M residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 192) chain M residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 193) chain T residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 194) chain T residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 195) chain G residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 196) chain G residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 197) chain H residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 198) chain B residue 172 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 199) chain H residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 200) chain L residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 201) chain L residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 202) chain K residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 203) chain K residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 204) chain J residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 205) chain J residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 206) chain I residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 207) chain I residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 208) chain D residue 172 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 209) chain N residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 210) chain O residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 211) chain O residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 212) chain P residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 213) chain P residue 57-77 type BINDING sequence LAFMEALTIYGLVVALALLFA description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 214) chain Q residue 3-23 type BINDING sequence PLIAAASVIAAGLAVGLASIG description BINDING => ECO:0000255|HAMAP-Rule:MF_01347 source Swiss-Prot : SWS_FT_FI1 215) chain E residue 363 type SITE sequence S description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 216) chain H residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 217) chain L residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 218) chain K residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 219) chain J residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 220) chain I residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 221) chain A residue 363 type SITE sequence S description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 222) chain C residue 363 type SITE sequence S description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 223) chain P residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 224) chain Q residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 225) chain R residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 226) chain M residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 227) chain T residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 228) chain G residue 61 type SITE sequence E description Required for activity => ECO:0000255|HAMAP-Rule:MF_01346 source Swiss-Prot : SWS_FT_FI2 229) chain a residue 185-194 type prosite sequence SLSFRLFGNI description ATPASE_A ATP synthase a subunit signature. SLSFRLFGNI source prosite : PS00449 230) chain d residue 207-226 type prosite sequence VRIKTVIDPSLVAGFTIRYG description ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. VrIktvIDpSLvAGFTIRyG source prosite : PS00389 231) chain S residue 40-61 type prosite sequence ARQPEAEGKIRGTLLLSLAFME description ATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE source prosite : PS00605 232) chain g residue 349-362 type prosite sequence ITGEILEIVAGANA description ATPASE_GAMMA ATP synthase gamma subunit signature. ITgEilEivaGAnA source prosite : PS00153 233) chain F residue 363-372 type prosite sequence PAVDPLDSTS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 234) chain E residue 356-365 type prosite sequence PAINVGISVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152

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