eF-site ID 1efr-ABCDEFG
PDB Code 1efr
Chain A, B, C, D, E, F, G

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Title BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN
Classification HYDROLASE/ANTIBIOTIC
Compound BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA
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 THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

2) chain B
residue 175
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

3) chain C
residue 175
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

4) chain D
residue 162
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

5) chain E
residue 162
type
sequence K
description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S.
source : PLP

6) chain F
residue 162
type
sequence K
description THE RESIDUE LISTED IS THE 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 C
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE MG C 601
source : AC3

16) chain D
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE MG D 601
source : AC4

17) chain D
residue 188
type
sequence E
description BINDING SITE FOR RESIDUE MG D 601
source : AC4

18) chain D
residue 189
type
sequence R
description BINDING SITE FOR RESIDUE MG D 601
source : AC4

19) chain F
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE MG F 601
source : AC5

20) chain F
residue 188
type
sequence E
description BINDING SITE FOR RESIDUE MG F 601
source : AC5

21) chain A
residue 170
type
sequence D
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

22) chain A
residue 171
type
sequence R
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

23) chain A
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

24) chain A
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

25) chain A
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

26) chain A
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

27) chain A
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

28) chain A
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

29) chain A
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

30) chain A
residue 362
type
sequence R
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

31) chain A
residue 363
type
sequence P
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

32) chain A
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

33) chain A
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ANP A 600
source : AC6

34) chain B
residue 171
type
sequence R
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

35) chain B
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

36) chain B
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

37) chain B
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

38) chain B
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

39) chain B
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

40) chain B
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

41) chain B
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

42) chain B
residue 362
type
sequence R
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

43) chain B
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

44) chain B
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ANP B 600
source : AC7

45) chain C
residue 170
type
sequence D
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

46) chain C
residue 171
type
sequence R
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

47) chain C
residue 172
type
sequence Q
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

48) chain C
residue 173
type
sequence T
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

49) chain C
residue 174
type
sequence G
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

50) chain C
residue 175
type
sequence K
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

51) chain C
residue 176
type
sequence T
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

52) chain C
residue 177
type
sequence S
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

53) chain C
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

54) chain C
residue 430
type
sequence Q
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

55) chain C
residue 431
type
sequence G
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

56) chain C
residue 432
type
sequence Q
description BINDING SITE FOR RESIDUE ANP C 600
source : AC8

57) chain C
residue 372
type
sequence S
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

58) chain C
residue 373
type
sequence R
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

59) chain D
residue 159
type
sequence G
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

60) chain D
residue 160
type
sequence V
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

61) chain D
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

62) chain D
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

63) chain D
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

64) chain D
residue 164
type
sequence V
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

65) chain D
residue 345
type
sequence Y
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

66) chain D
residue 418
type
sequence F
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

67) chain D
residue 421
type
sequence A
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

68) chain D
residue 424
type
sequence F
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

69) chain D
residue 425
type
sequence T
description BINDING SITE FOR RESIDUE ADP D 600
source : AC9

70) chain B
residue 344
type
sequence S
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

71) chain B
residue 371
type
sequence V
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

72) chain B
residue 373
type
sequence R
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

73) chain F
residue 158
type
sequence A
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

74) chain F
residue 159
type
sequence G
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

75) chain F
residue 160
type
sequence V
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

76) chain F
residue 161
type
sequence G
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

77) chain F
residue 162
type
sequence K
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

78) chain F
residue 163
type
sequence T
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

79) chain F
residue 164
type
sequence V
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

80) chain F
residue 189
type
sequence R
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

81) chain F
residue 345
type
sequence Y
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

82) chain F
residue 418
type
sequence F
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

83) chain F
residue 421
type
sequence A
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

84) chain F
residue 424
type
sequence F
description BINDING SITE FOR RESIDUE ANP F 600
source : BC1

85) chain A
residue 331
type
sequence A
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

86) chain A
residue 332
type
sequence G
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

87) chain A
residue 333
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

88) chain A
residue 334
type
sequence V
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

89) chain A
residue 335
type
sequence S
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

90) chain A
residue 349
type
sequence Q
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

91) chain A
residue 351
type
sequence F
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

92) chain A
residue 369
type
sequence L
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

93) chain B
residue 171
type
sequence R
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

94) chain B
residue 354
type
sequence T
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

95) chain B
residue 358
type
sequence Y
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

96) chain E
residue 155
type
sequence F
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

97) chain E
residue 315
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

98) chain E
residue 317
type
sequence L
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

99) chain E
residue 332
type
sequence T
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

100) chain E
residue 352
type
sequence D
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

101) chain G
residue 7
type
sequence T
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

102) chain G
residue 250
type
sequence F
description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C
source : BC2

103) chain D
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA1

104) chain D
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA1

105) chain D
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA1

106) chain E
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA2

107) chain E
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA2

108) chain E
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA2

109) chain F
residue 162
type catalytic
sequence K
description 178
source MCSA : MCSA3

110) chain F
residue 188
type catalytic
sequence E
description 178
source MCSA : MCSA3

111) chain F
residue 189
type catalytic
sequence R
description 178
source MCSA : MCSA3

112) chain A
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

113) chain B
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

114) chain C
residue 161
type MOD_RES
sequence R
description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265
source Swiss-Prot : SWS_FT_FI10

115) chain G
residue 14
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

116) chain E
residue 157
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

117) chain F
residue 157
type MOD_RES
sequence G
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

118) chain B
residue 430
type MOD_RES
sequence Q
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

119) chain C
residue 170
type MOD_RES
sequence D
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

120) chain C
residue 430
type MOD_RES
sequence Q
description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI1

121) chain G
residue 24
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI2

122) chain G
residue 245
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI2

123) chain F
residue 189
type MOD_RES
sequence R
description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI2

124) chain G
residue 30
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

125) chain E
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

126) chain F
residue 74
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

127) chain F
residue 111
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

128) chain F
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

129) chain F
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

130) chain F
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

131) chain D
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

132) chain D
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

133) chain D
residue 472
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

134) chain E
residue 74
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

135) chain E
residue 111
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

136) chain E
residue 209
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

137) chain E
residue 214
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI3

138) chain G
residue 90
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

139) chain C
residue 22
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

140) chain C
residue 123
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

141) chain C
residue 141
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

142) chain E
residue 148
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

143) chain E
residue 376
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

144) chain F
residue 148
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

145) chain F
residue 376
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

146) chain B
residue 123
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

147) chain B
residue 141
type MOD_RES
sequence S
description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2
source Swiss-Prot : SWS_FT_FI4

148) chain E
residue 262
type MOD_RES
sequence T
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

149) chain F
residue 262
type MOD_RES
sequence T
description Phosphoserine => ECO:0000250|UniProtKB:P36542
source Swiss-Prot : SWS_FT_FI5

150) chain D
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

151) chain E
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

152) chain F
residue 365
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P06576
source Swiss-Prot : SWS_FT_FI6

153) chain D
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

154) chain D
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

155) chain E
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

156) chain E
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

157) chain F
residue 430
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

158) chain F
residue 435
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P56480
source Swiss-Prot : SWS_FT_FI8

159) chain D
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

160) chain A
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

161) chain A
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

162) chain B
residue 118
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

163) chain B
residue 124
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

164) chain B
residue 187
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

165) chain B
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

166) chain B
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

167) chain B
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

168) chain B
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

169) chain B
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

170) chain E
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

171) chain B
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

172) chain B
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

173) chain B
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

174) chain C
residue 118
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

175) chain C
residue 124
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

176) chain C
residue 187
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

177) chain C
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

178) chain C
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

179) chain C
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

180) chain C
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

181) chain F
residue 56
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

182) chain C
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

183) chain C
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

184) chain C
residue 488
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

185) chain C
residue 496
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

186) chain A
residue 196
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

187) chain A
residue 218
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

188) chain A
residue 262
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

189) chain A
residue 384
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

190) chain A
residue 455
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

191) chain A
residue 463
type CARBOHYD
sequence K
description O-linked (GlcNAc) serine => ECO:0000250
source Swiss-Prot : SWS_FT_FI9

192) chain A
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

193) chain B
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

194) chain C
residue 391
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P25705
source Swiss-Prot : SWS_FT_FI11

195) chain A
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

196) chain B
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

197) chain C
residue 33
type CARBOHYD
sequence S
description O-linked (GlcNAc) serine; alternate => ECO:0000250
source Swiss-Prot : SWS_FT_FI12

198) chain D
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

199) chain B
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

200) chain C
residue 80
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

201) chain C
residue 83
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

202) chain C
residue 89
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

203) chain C
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

204) chain C
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

205) chain E
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

206) chain F
residue 383
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

207) chain A
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

208) chain A
residue 498
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

209) chain B
residue 80
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

210) chain B
residue 83
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

211) chain B
residue 89
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

212) chain B
residue 197
type MOD_RES
sequence K
description Phosphoserine => ECO:0000250|UniProtKB:P10719
source Swiss-Prot : SWS_FT_FI7

213) chain G
residue 258-271
type prosite
sequence ITKELIEIISGAAA
description ATPASE_GAMMA ATP synthase gamma subunit signature. ITkEliEiisGAaA
source prosite : PS00153

214) chain A
residue 363-372
type prosite
sequence PAINVGLSVS
description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS
source prosite : PS00152

215) 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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