eF-site ID 3zk1-ABCDEFGHIJKLMNOPQRSTUV
PDB Code 3zk1
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V

click to enlarge
Title Crystal structure of the sodium binding rotor ring at pH 5.3
Classification MEMBRANE PROTEIN
Compound ATP SYNTHASE SUBUNIT C
Source Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131) (ATPL_FUSNN)
Sequence A:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
B:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
C:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
D:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
E:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
F:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
G:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
H:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
I:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
J:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
K:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
L:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
M:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
N:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
O:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
P:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
Q:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
R:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
S:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
T:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
U:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
V:  MDLLTAKTIVLGCSAVGAGLAMIAGLGPGIGEGYAAGKAV
ESVARQPEARGSIISTMILGQAVAESTGIYSLVIALILLY
ANPFLSKLG
Description


Functional site

1) chain A
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA A 90
source : AC1

2) chain A
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA A 90
source : AC1

3) chain K
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA A 90
source : AC1

4) chain K
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA A 90
source : AC1

5) chain A
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU A 92
source : AC2

6) chain A
residue 16
type
sequence V
description BINDING SITE FOR RESIDUE DMU A 92
source : AC2

7) chain K
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU A 92
source : AC2

8) chain K
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU A 92
source : AC2

9) chain A
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA B 90
source : AC3

10) chain A
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA B 90
source : AC3

11) chain B
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA B 90
source : AC3

12) chain B
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA B 90
source : AC3

13) chain A
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU B 92
source : AC4

14) chain A
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU B 92
source : AC4

15) chain B
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA C 90
source : AC5

16) chain B
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA C 90
source : AC5

17) chain C
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA C 90
source : AC5

18) chain C
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA C 90
source : AC5

19) chain B
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU C 92
source : AC6

20) chain C
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA D 90
source : AC7

21) chain C
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA D 90
source : AC7

22) chain D
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA D 90
source : AC7

23) chain D
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA D 90
source : AC7

24) chain C
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU D 92
source : AC8

25) chain D
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU D 92
source : AC8

26) chain D
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU D 92
source : AC8

27) chain D
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU D 92
source : AC8

28) chain D
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA E 90
source : AC9

29) chain D
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA E 90
source : AC9

30) chain E
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA E 90
source : AC9

31) chain E
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA E 90
source : AC9

32) chain D
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU E 92
source : BC1

33) chain D
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU E 92
source : BC1

34) chain E
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU E 92
source : BC1

35) chain E
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU E 92
source : BC1

36) chain E
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU E 92
source : BC1

37) chain E
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA F 90
source : BC2

38) chain E
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA F 90
source : BC2

39) chain F
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA F 90
source : BC2

40) chain F
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA F 90
source : BC2

41) chain E
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU F 92
source : BC3

42) chain E
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU F 92
source : BC3

43) chain F
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU F 92
source : BC3

44) chain F
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA G 90
source : BC4

45) chain F
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA G 90
source : BC4

46) chain G
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA G 90
source : BC4

47) chain G
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA G 90
source : BC4

48) chain F
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

49) chain F
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

50) chain F
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

51) chain G
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

52) chain G
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

53) chain G
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU G 92
source : BC5

54) chain G
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA H 90
source : BC6

55) chain G
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA H 90
source : BC6

56) chain H
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA H 90
source : BC6

57) chain H
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA H 90
source : BC6

58) chain G
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

59) chain G
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

60) chain H
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

61) chain H
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

62) chain H
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

63) chain H
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU H 92
source : BC7

64) chain H
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA I 90
source : BC8

65) chain H
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA I 90
source : BC8

66) chain I
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA I 90
source : BC8

67) chain I
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA I 90
source : BC8

68) chain H
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU I 92
source : BC9

69) chain H
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU I 92
source : BC9

70) chain I
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU I 92
source : BC9

71) chain I
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU I 92
source : BC9

72) chain I
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA J 90
source : CC1

73) chain I
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA J 90
source : CC1

74) chain J
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA J 90
source : CC1

75) chain J
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA J 90
source : CC1

76) chain J
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU J 92
source : CC2

77) chain J
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU J 92
source : CC2

78) chain J
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA K 90
source : CC3

79) chain J
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA K 90
source : CC3

80) chain K
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA K 90
source : CC3

81) chain K
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA K 90
source : CC3

82) chain J
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU K 92
source : CC4

83) chain K
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU K 92
source : CC4

84) chain K
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU K 92
source : CC4

85) chain L
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA L 90
source : CC5

86) chain L
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA L 90
source : CC5

87) chain V
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA L 90
source : CC5

88) chain V
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA L 90
source : CC5

89) chain L
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU L 92
source : CC6

90) chain V
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU L 92
source : CC6

91) chain L
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA M 90
source : CC7

92) chain L
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA M 90
source : CC7

93) chain M
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA M 90
source : CC7

94) chain M
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA M 90
source : CC7

95) chain L
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU M 92
source : CC8

96) chain L
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU M 92
source : CC8

97) chain L
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU M 92
source : CC8

98) chain M
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU M 92
source : CC8

99) chain M
residue 87
type
sequence K
description BINDING SITE FOR RESIDUE TAM M 1090
source : CC9

100) chain N
residue 80
type
sequence Y
description BINDING SITE FOR RESIDUE TAM M 1090
source : CC9

101) chain M
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA N 90
source : DC1

102) chain M
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA N 90
source : DC1

103) chain N
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA N 90
source : DC1

104) chain N
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA N 90
source : DC1

105) chain M
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

106) chain M
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

107) chain N
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

108) chain N
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

109) chain N
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

110) chain N
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU N 92
source : DC2

111) chain N
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA O 90
source : DC3

112) chain N
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA O 90
source : DC3

113) chain O
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA O 90
source : DC3

114) chain O
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA O 90
source : DC3

115) chain N
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

116) chain N
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

117) chain O
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

118) chain O
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

119) chain O
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

120) chain O
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU O 92
source : DC4

121) chain O
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA P 90
source : DC5

122) chain O
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA P 90
source : DC5

123) chain P
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA P 90
source : DC5

124) chain P
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA P 90
source : DC5

125) chain O
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU P 92
source : DC6

126) chain O
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU P 92
source : DC6

127) chain P
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU P 92
source : DC6

128) chain P
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU P 92
source : DC6

129) chain P
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA Q 90
source : DC7

130) chain P
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA Q 90
source : DC7

131) chain Q
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA Q 90
source : DC7

132) chain Q
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA Q 90
source : DC7

133) chain P
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU Q 92
source : DC8

134) chain P
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU Q 92
source : DC8

135) chain Q
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA R 90
source : DC9

136) chain Q
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA R 90
source : DC9

137) chain R
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA R 90
source : DC9

138) chain R
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA R 90
source : DC9

139) chain Q
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU R 92
source : EC1

140) chain R
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU R 92
source : EC1

141) chain R
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU R 92
source : EC1

142) chain Q
residue 59
type
sequence L
description BINDING SITE FOR RESIDUE TAM R 1090
source : EC2

143) chain R
residue 50
type
sequence R
description BINDING SITE FOR RESIDUE TAM R 1090
source : EC2

144) chain R
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA S 90
source : EC3

145) chain R
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA S 90
source : EC3

146) chain S
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA S 90
source : EC3

147) chain S
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA S 90
source : EC3

148) chain R
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU S 92
source : EC4

149) chain R
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU S 92
source : EC4

150) chain S
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU S 92
source : EC4

151) chain S
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU S 92
source : EC4

152) chain S
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU S 92
source : EC4

153) chain S
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA T 90
source : EC5

154) chain S
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA T 90
source : EC5

155) chain T
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA T 90
source : EC5

156) chain T
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA T 90
source : EC5

157) chain S
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU T 92
source : EC6

158) chain S
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU T 92
source : EC6

159) chain T
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU T 92
source : EC6

160) chain T
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU T 92
source : EC6

161) chain T
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA U 90
source : EC7

162) chain T
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA U 90
source : EC7

163) chain U
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA U 90
source : EC7

164) chain U
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA U 90
source : EC7

165) chain T
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

166) chain T
residue 9
type
sequence I
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

167) chain U
residue 1
type
sequence M
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

168) chain U
residue 2
type
sequence D
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

169) chain U
residue 5
type
sequence T
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

170) chain U
residue 16
type
sequence V
description BINDING SITE FOR RESIDUE DMU U 92
source : EC8

171) chain U
residue 63
type
sequence V
description BINDING SITE FOR RESIDUE NA V 90
source : EC9

172) chain U
residue 66
type
sequence S
description BINDING SITE FOR RESIDUE NA V 90
source : EC9

173) chain V
residue 32
type
sequence E
description BINDING SITE FOR RESIDUE NA V 90
source : EC9

174) chain V
residue 65
type
sequence E
description BINDING SITE FOR RESIDUE NA V 90
source : EC9

175) chain U
residue 13
type
sequence C
description BINDING SITE FOR RESIDUE DMU V 92
source : FC1

176) chain A
residue 70
type
sequence Y
description BINDING SITE FOR RESIDUE LMT B 1090
source : FC2

177) chain C
residue 80
type
sequence Y
description BINDING SITE FOR RESIDUE LMT C 1090
source : FC3

178) chain C
residue 69
type
sequence I
description BINDING SITE FOR RESIDUE LMT C 1091
source : FC4

179) chain C
residue 73
type
sequence V
description BINDING SITE FOR RESIDUE LMT C 1091
source : FC4

180) chain C
residue 81
type
sequence A
description BINDING SITE FOR RESIDUE LMT C 1091
source : FC4

181) chain A
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

182) chain E
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

183) chain F
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

184) chain F
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

185) chain G
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

186) chain G
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

187) chain H
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

188) chain H
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

189) chain I
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

190) chain I
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

191) chain J
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

192) chain A
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

193) chain J
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

194) chain K
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

195) chain K
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

196) chain L
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

197) chain L
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

198) chain M
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

199) chain M
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

200) chain N
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

201) chain N
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

202) chain O
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

203) chain B
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

204) chain O
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

205) chain P
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

206) chain P
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

207) chain Q
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

208) chain Q
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

209) chain R
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

210) chain R
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

211) chain S
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

212) chain S
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

213) chain T
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

214) chain B
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

215) chain T
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

216) chain U
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

217) chain U
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

218) chain V
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

219) chain V
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

220) chain C
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

221) chain C
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

222) chain D
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

223) chain D
residue 58-78
type TRANSMEM
sequence ILGQAVAESTGIYSLVIALIL
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

224) chain E
residue 9-29
type TRANSMEM
sequence IVLGCSAVGAGLAMIAGLGPG
description Helical => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI1

225) chain A
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

226) chain J
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

227) chain K
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

228) chain L
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

229) chain M
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

230) chain N
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

231) chain O
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

232) chain P
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

233) chain Q
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

234) chain R
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

235) chain S
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

236) chain B
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

237) chain T
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

238) chain U
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

239) chain V
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

240) chain C
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

241) chain D
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

242) chain E
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

243) chain F
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

244) chain G
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

245) chain H
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

246) chain I
residue 65
type SITE
sequence E
description Reversibly protonated during proton transport => ECO:0000255|HAMAP-Rule:MF_01396
source Swiss-Prot : SWS_FT_FI2

247) chain A
residue 44-65
type prosite
sequence ARQPEARGSIISTMILGQAVAE
description ATPASE_C ATP synthase c subunit signature. ARQPeargsIiStmILgqaVaE
source prosite : PS00605


Display surface

Download
Links