eF-site ID 2wpd-ABCDEFGHIJKLMNOPQRS PDB Code 2wpd Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S click to enlarge Title The Mg.ADP inhibited state of the yeast F1c10 ATP synthase Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL Source ORGANISM_COMMON: BAKER'S YEAST; ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE; Sequence A:  NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMA LNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGL LGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVH EPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTI LNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKH ALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHS RLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVI SITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAL KQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGER LTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGE FESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATES FVATF B:  ANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGM ALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPG LLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSV HEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDT ILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQ HDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGK HALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLH SRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNV ISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKA LKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGE RLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIG EFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATE SFVAT C:  NLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMA LNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGL LGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVH EPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTI LNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQH DAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKH ALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHS RLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVI SITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKAL KQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGER LTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGE FESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATES FVATF D:  STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGK LVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISV PVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTV FIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETG VINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTL ATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATT FAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQ EHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVE RARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVL EGKYDNIPEHAFYMVGGIEDVVAKAEKLAA E:  STPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGK LVLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISV PVGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFA EQSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTV FIQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETG VINLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRD EEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTL ATDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATT FAHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQ EHYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVE RARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVL EGKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN F:  TPITGKVTAVIGAIVDVHFEQSELPAILNALEIKTPQGKL VLEVAQHLGENTVRTIAMDGTEGLVRGEKVLDTGGPISVP VGRETLGRIINVIGEPIDERGPIKSKLRKPIHADPPSFAE QSTSAEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVF IQELINNIAKAHGGFSVFTGVGERTREGNDLYREMKETGV INLEGESKVALVFGQMNEPPGARARVALTGLTIAEYFRDE EGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLA TDMGLLQERITTTKKGSVTSVQAVYVPADDLTDPAPATTF AHLDATTVLSRGISELGIYPAVDPLDSKSRLLDAAVVGQE HYDVASKVQETLQTYKSLQDIIAILGMDELSEQDKLTVER ARKIQRFLSQPFAVAEVFTGIPGKLVRLKDTVASFKAVLE GKYDNIPEHAFYMVGGIEDVVAKAEKLAAEAN G:  ATLKEVEMRLKSIKNIEKITKTMKIVASTRLSKAEKAKIS AKKMDEAEQLFYKNAETKNLDKELIVAITSDKGLCGSIHS QLAKAVRRHLNDQPNADIVTIGDKIKMQLLRTHPNNIKLS INGIGKDAPTFQESALIADKLLSVMKAGTYPKISIFYNDP VSSLSFEPSEKPIFNAKTIEQSPSFGKFEIDTDANVPRDL FEYTLANQMLTAMAQGYAAEISARRNAMDNASKNAGDMIN RYSILYNRTRQAVITNELVDIITGASSLG H:  SSGLKLQFALPHETLYSGSEVTQVNLPAKSGRIGVLANHV PTVEQLLPGVVEVMEGSNSKKFFISGGFATVQPDSQLCVT AIEAFPLESFSQENIKNLLAEAKKNVSSSDAREAAEAAIQ VEVLENLQSVLK I:  SAWRKAGISYAAYLNVAAQAIRSSLKTELQTASVLNRSQT DAFYTQYKNGTAASEPTPI J:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV K:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV L:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV M:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV N:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV O:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV P:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV Q:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV R:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV S:  MQLVLAAKYIGAGISTIGLLGAGIGIAIVFAALINGVSRN PSIKDTVFPMAILGFALSEATGLFCLMVSFLLLFGV Description Functional site 1) chain A residue 174 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 2) chain A residue 175 type sequence T description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 3) chain A residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 4) chain A residue 177 type sequence K description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 5) chain A residue 178 type sequence T description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 6) chain A residue 179 type sequence A description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 7) chain A residue 330 type sequence E description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 8) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 9) chain A residue 434 type sequence Q description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 10) chain D residue 355 type sequence S description BINDING SITE FOR RESIDUE ATP A 600 source : AC1 11) chain A residue 178 type sequence T description BINDING SITE FOR RESIDUE MG A 601 source : AC2 12) chain A residue 271 type sequence D description BINDING SITE FOR RESIDUE MG A 601 source : AC2 13) chain B residue 174 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 14) chain B residue 175 type sequence T description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 15) chain B residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 16) chain B residue 177 type sequence K description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 17) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 18) chain B residue 179 type sequence A description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 19) chain B residue 364 type sequence R description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 20) chain B residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 21) chain B residue 434 type sequence Q description BINDING SITE FOR RESIDUE ATP B 600 source : AC3 22) chain B residue 177 type sequence K description BINDING SITE FOR RESIDUE MG B 601 source : AC4 23) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE MG B 601 source : AC4 24) chain B residue 271 type sequence D description BINDING SITE FOR RESIDUE MG B 601 source : AC4 25) chain C residue 174 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 26) chain C residue 176 type sequence G description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 27) chain C residue 177 type sequence K description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 28) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 29) chain C residue 179 type sequence A description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 30) chain C residue 364 type sequence R description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 31) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 32) chain C residue 434 type sequence Q description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 33) chain F residue 355 type sequence S description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 34) chain F residue 368 type sequence Y description BINDING SITE FOR RESIDUE ATP C 600 source : AC5 35) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE MG C 601 source : AC6 36) chain C residue 271 type sequence D description BINDING SITE FOR RESIDUE MG C 601 source : AC6 37) chain C residue 375 type sequence R description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 38) chain D residue 158 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 39) chain D residue 159 type sequence A description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 40) chain D residue 160 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 41) chain D residue 161 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 42) chain D residue 162 type sequence G description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 43) chain D residue 163 type sequence K description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 44) chain D residue 164 type sequence T description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 45) chain D residue 165 type sequence V description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 46) chain D residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 47) chain D residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP D 600 source : AC7 48) chain D residue 164 type sequence T description BINDING SITE FOR RESIDUE MG D 601 source : AC8 49) chain D residue 189 type sequence E description BINDING SITE FOR RESIDUE MG D 601 source : AC8 50) chain B residue 373 type sequence V description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 51) chain B residue 374 type sequence S description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 52) chain B residue 375 type sequence R description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 53) chain F residue 160 type sequence G description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 54) chain F residue 162 type sequence G description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 55) chain F residue 163 type sequence K description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 56) chain F residue 164 type sequence T description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 57) chain F residue 165 type sequence V description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 58) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 59) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP F 600 source : AC9 60) chain F residue 164 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : BC1 61) chain F residue 189 type sequence E description BINDING SITE FOR RESIDUE MG F 601 source : BC1 62) chain F residue 256 type sequence D description BINDING SITE FOR RESIDUE MG F 601 source : BC1 63) chain G residue 263-276 type prosite sequence ITNELVDIITGASS description ATPASE_GAMMA ATP synthase gamma subunit signature. ITnElvDiitGAsS source prosite : PS00153 64) chain J residue 38-59 type prosite sequence SRNPSIKDTVFPMAILGFALSE description ATPASE_C ATP synthase c subunit signature. SRNPsikdtVfPmaILgfaLsE source prosite : PS00605 65) chain A residue 365-374 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152 66) chain D residue 346-355 type prosite sequence PAVDPLDSKS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152 67) chain J residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 68) chain N residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 69) chain O residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 70) chain O residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 71) chain P residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 72) chain P residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 73) chain Q residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 74) chain Q residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 75) chain R residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 76) chain R residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 77) chain S residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 78) chain J residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 79) chain S residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 80) chain K residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 81) chain K residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 82) chain L residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 83) chain L residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 84) chain M residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 85) chain M residue 52-72 type TRANSMEM sequence ILGFALSEATGLFCLMVSFLL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 86) chain N residue 14-34 type TRANSMEM sequence ISTIGLLGAGIGIAIVFAALI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 87) chain J residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 88) chain S residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 89) chain K residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 90) chain L residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 91) chain M residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 92) chain N residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 93) chain O residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 94) chain P residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 95) chain Q residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 96) chain R residue 59 type SITE sequence E description Reversibly protonated during proton transport => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 97) chain J residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 98) chain S residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 99) chain K residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 100) chain L residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 101) chain M residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 102) chain N residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 103) chain O residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 104) chain P residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 105) chain Q residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3 106) chain R residue 1 type MOD_RES sequence M description N-formylmethionine => ECO:0000269|PubMed:2894987 source Swiss-Prot : SWS_FT_FI3

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