eF-site ID 6fkh-ABCDEFGHIJKLMNOPQRSTabdegp
PDB Code 6fkh
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 2
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
TEEAEALLKEAIQEQMERFLLQ
B:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG
QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA
PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA
PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV
GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM
KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM
AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV
GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD
PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ
PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE
DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR
GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL
C:  IRADEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIH
GLDEVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMI
QEGSSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEIT
ASESRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRG
QRELIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKA
SSVAQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTG
AALAEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPG
REAYPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQ
AGDVSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGIS
VSRVGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDL
DKATQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTN
GYLDSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFT
EEAEALLKEAIQEQMERFLLQ
D:  KNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAGQ
PMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGAP
LSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSAP
AFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVG
KTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMK
ESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTMA
EYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVG
YQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTDP
APATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQP
RIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEED
RLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRG
FQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMESKL
E:  DEISKIIRERIEGYNREVKVVNTGTVLQVGDGIARIHGLD
EVMAGELVEFEEGTIGIALNLESNNVGVVLMGDGLMIQEG
SSVKATGRIAQIPVSEAYLGRVINALAKPIDGRGEITASE
SRLIESPAPGIMSRRSVYEPLQTGLIAIDAMIPVGRGQRE
LIIGDRQTGKTAVATDTILNQQGQNVICVYVAIGQKASSV
AQVVTNFQERGAMEYTIVVAETADSPATLQYLAPYTGAAL
AEYFMYRERHTLIIYDDLSKQAQAYRQMSLLLRRPPGREA
YPGDVFYLHSRLLERAAKLSSLLGEGSMTALPIVETQAGD
VSAYIPTNVISITDGQIFLSADLFNAGIRPAINVGISVSR
VGSAAQIKAMKKVAGKLKLELAQFAELEAFAQFASDLDKA
TQNQLARGQRLRELLKQPQSAPLTVEEQVMTIYTGTNGYL
DSLELDQVRKYLVELRTYVKTNKPEFQEIISSTKTFTEEA
EALLKEAIQEQMERFLL
F:  KKNLGRIAQIIGPVLDVAFPPGKMPNIYNALIVKGRDTAG
QPMNVTCEVQQLLGNNRVRAVAMSATDGLTRGMEVIDTGA
PLSVPVGGATLGRIFNVLGEPVDNLGPVDTRTTSPIHRSA
PAFTQLDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGV
GKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEM
KESGVINEQNIAESKVALVYGQMNEPPGARMRVGLTALTM
AEYFRDVNEQDVLLFIDNIFRFVQAGSEVSALLGRMPSAV
GYQPTLSTEMGSLQERITSTKEGSITSIQAVYVPADDLTD
PAPATTFAHLDATTVLSRGLAAKGIYPAVDPLDSTSTMLQ
PRIVGEEHYEIAQRVKETLQRYKELQDIIAILGLDELSEE
DRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIR
GFQLILSGELDSLPEQAFYLVGNIDEATAKAMNLEMES
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 alpha, chloroplastic (E.C.3.6.3.14), ATP synthase subunit beta, chloroplastic (E.C.3.6.3.14), ATP synthase epsilon chain, chloroplastic, ATP synthase gamma chain, chloroplastic, ATP synthase subunit c, chloroplastic, ATP synthase subunit b', chloroplastic, ATP synthase subunit b, chloroplastic, ATP synthase delta chain, chloroplastic


Functional site

1) chain D
residue 363-372
type prosite
sequence PAVDPLDSTS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
source prosite : PS00152

2) chain C
residue 356-365
type prosite
sequence PAINVGISVS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS
source prosite : PS00152

3) chain g
residue 349-362
type prosite
sequence ITGEILEIVAGANA
description ATPASE_GAMMA ATP synthase gamma subunit signature. ITgEilEivaGAnA
source prosite : PS00153

4) chain d
residue 207-226
type prosite
sequence VRIKTVIDPSLVAGFTIRYG
description ATPASE_DELTA ATP synthase delta (OSCP) subunit signature. VrIktvIDpSLvAGFTIRyG
source prosite : PS00389

5) chain a
residue 185-194
type prosite
sequence SLSFRLFGNI
description ATPASE_A ATP synthase a subunit signature. SLSFRLFGNI
source prosite : PS00449

6) chain S
residue 40-61
type prosite
sequence ARQPEAEGKIRGTLLLSLAFME
description ATPASE_C ATP synthase c subunit signature. ARQPeaegkIrGtlLLslaFmE
source prosite : PS00605

7) chain b
residue 27-49
type TRANSMEM
sequence LATNLINLSVVLGVLIFFGKGVL
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

8) chain Q
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

9) chain R
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

10) chain R
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

11) chain M
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

12) chain M
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

13) chain T
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

14) chain T
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

15) chain G
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

16) chain G
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

17) chain H
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

18) chain S
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

19) chain H
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

20) chain L
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

21) chain L
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

22) chain K
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

23) chain K
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

24) chain J
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

25) chain J
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

26) chain I
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

27) chain I
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

28) chain N
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

29) chain N
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

30) chain O
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

31) chain O
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

32) chain P
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

33) chain P
residue 57-77
type TRANSMEM
sequence LAFMEALTIYGLVVALALLFA
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

34) chain Q
residue 3-23
type TRANSMEM
sequence PLIAAASVIAAGLAVGLASIG
description Helical => ECO:0000255|HAMAP-Rule:MF_01398
source Swiss-Prot : SWS_FT_FI1

35) 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

36) 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

37) 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

38) 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

39) 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

40) 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

41) 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

42) 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

43) 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

44) 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

45) 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

46) 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

47) 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

48) 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


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