eF-site ID 3ze3-ABCDEF
PDB Code 3ze3
Chain A, B, C, D, E, F

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Title Crystal structure of the integral membrane diacylglycerol kinase - delta7
Classification TRANSFERASE
Compound DIACYLGLYCEROL KINASE
Source (KDGL_ECOLI)
Sequence A:  GFTRIIKAAGYSWKGLRAAWINEAAFRQEGVAVLLCVVIA
AWLDVDAVTRVLLISSVMLVMIVELLNSAIEAVVDRIGSE
YHELSGRAKDLGSAAVLIAIIDAVITWAILLWSHFG
B:  AWINEAAFRQEGVAVLLCVVIAAWLDVDAVTRVLLISSVM
LVMIVELLNSAIEAVVDRIGSEYHELSGRAKDLGSAAVLI
AIIDAVITWAILLWSHFG
C:  RQEGVAVLLCVVIAAWLDVDAVTRVLLISSVMLVMIVELL
NSAIEAVVDRIGSEYHELSGRAKDLGSAAVLIAIIDAVIT
WAILLWSHFG
D:  AGYSWKGLRAAWINEAAFRQEGVAVLLCVVIAAWLDVDAV
TRVLLISSVMLVMIVELLNSAIEAVVDRIGSEYHELSGRA
KDLGSAAVLIAIIDAVITWAILLWSHFG
E:  VAVLLCVVIAAVDAVTRVLLISSVMLVMIVELLNSAIEAV
VDRIGSEYHELSGRAKDLGSAAVLIAIIDAVITWAILLWS
HFG
F:  EGVAVLLCVVIAAWLDVDAVTRVLLISSVMLVMIVELLNS
AIEAVVDRIGSEYHELSGRAKDLGSAAVLIAIIDAVITWA
ILLWSHFG
Description


Functional site

1) chain D
residue 64
type
sequence L
description BINDING SITE FOR RESIDUE NA F 1122
source : AC1

2) chain D
residue 107
type
sequence D
description BINDING SITE FOR RESIDUE NA F 1122
source : AC1

3) chain F
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE NA F 1122
source : AC1

4) chain F
residue 64
type
sequence L
description BINDING SITE FOR RESIDUE NA F 1122
source : AC1

5) chain D
residue 60
type
sequence S
description BINDING SITE FOR RESIDUE NA E 1122
source : AC2

6) chain E
residue 61
type
sequence S
description BINDING SITE FOR RESIDUE NA E 1122
source : AC2

7) chain E
residue 111
type
sequence T
description BINDING SITE FOR RESIDUE NA E 1122
source : AC2

8) chain D
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 1122
source : AC3

9) chain D
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ZN D 1122
source : AC3

10) chain D
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE FLC D 1123
source : AC4

11) chain D
residue 28
type
sequence E
description BINDING SITE FOR RESIDUE ACT D 1124
source : AC5

12) chain D
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE ACT D 1124
source : AC5

13) chain D
residue 72
type
sequence N
description BINDING SITE FOR RESIDUE ACT D 1124
source : AC5

14) chain D
residue 73
type
sequence S
description BINDING SITE FOR RESIDUE ACT D 1124
source : AC5

15) chain D
residue 76
type
sequence E
description BINDING SITE FOR RESIDUE ACT D 1124
source : AC5

16) chain A
residue 13
type
sequence A
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

17) chain A
residue 14
type
sequence A
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

18) chain A
residue 17
type
sequence S
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

19) chain B
residue 98
type
sequence S
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

20) chain B
residue 101
type
sequence V
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

21) chain B
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

22) chain B
residue 105
type
sequence I
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

23) chain B
residue 110
type
sequence I
description BINDING SITE FOR RESIDUE 78N B 1122
source : AC6

24) chain A
residue 9
type
sequence R
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

25) chain B
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

26) chain B
residue 65
type
sequence V
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

27) chain B
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

28) chain B
residue 108
type
sequence A
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

29) chain B
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

30) chain B
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE 78N B 1123
source : AC7

31) chain A
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

32) chain A
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

33) chain C
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

34) chain D
residue 25
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

35) chain D
residue 29
type
sequence A
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

36) chain D
residue 32
type
sequence R
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

37) chain D
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

38) chain D
residue 36
type
sequence V
description BINDING SITE FOR RESIDUE 78M D 1125
source : AC8

39) chain B
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

40) chain B
residue 55
type
sequence R
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

41) chain C
residue 110
type
sequence I
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

42) chain C
residue 114
type
sequence I
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

43) chain C
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

44) chain C
residue 118
type
sequence S
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

45) chain D
residue 33
type
sequence Q
description BINDING SITE FOR RESIDUE 78N C 1122
source : AC9

46) chain A
residue 18
type
sequence W
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

47) chain A
residue 22
type
sequence R
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

48) chain A
residue 25
type
sequence W
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

49) chain A
residue 26
type
sequence I
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

50) chain A
residue 39
type
sequence L
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

51) chain A
residue 63
type
sequence M
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

52) chain A
residue 66
type
sequence M
description BINDING SITE FOR RESIDUE 78N A 1122
source : BC1

53) chain A
residue 30
type
sequence A
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

54) chain A
residue 31
type
sequence F
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

55) chain A
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

56) chain A
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

57) chain A
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

58) chain A
residue 105
type
sequence I
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

59) chain D
residue 22
type
sequence R
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

60) chain D
residue 25
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1126
source : BC2

61) chain B
residue 47
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1127
source : BC3

62) chain D
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE 78M D 1127
source : BC3

63) chain D
residue 109
type
sequence V
description BINDING SITE FOR RESIDUE 78M D 1127
source : BC3

64) chain D
residue 113
type
sequence A
description BINDING SITE FOR RESIDUE 78M D 1127
source : BC3

65) chain A
residue 40
type
sequence L
description BINDING SITE FOR RESIDUE 78N C 1123
source : BC4

66) chain A
residue 47
type
sequence W
description BINDING SITE FOR RESIDUE 78N C 1123
source : BC4

67) chain C
residue 34
type
sequence E
description BINDING SITE FOR RESIDUE 78N C 1123
source : BC4

68) chain C
residue 69
type
sequence E
description BINDING SITE FOR RESIDUE 78N C 1123
source : BC4

69) chain C
residue 112
type
sequence W
description BINDING SITE FOR RESIDUE 78N C 1123
source : BC4

70) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

71) chain B
residue 35
type
sequence G
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

72) chain B
residue 36
type
sequence V
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

73) chain D
residue 47
type
sequence W
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

74) chain D
residue 48
type
sequence L
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

75) chain D
residue 49
type
sequence D
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

76) chain D
residue 120
type
sequence F
description BINDING SITE FOR RESIDUE 78M D 1128
source : BC5

77) chain A
residue 42
type
sequence V
description BINDING SITE FOR RESIDUE 78N A 1123
source : BC6

78) chain A
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE 78N A 1123
source : BC6

79) chain A
residue 55
type
sequence R
description BINDING SITE FOR RESIDUE 78N A 1123
source : BC6

80) chain A
residue 50
type
sequence V
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

81) chain A
residue 51
type
sequence D
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

82) chain A
residue 52
type
sequence A
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

83) chain A
residue 55
type
sequence R
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

84) chain B
residue 114
type
sequence I
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

85) chain B
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 78N A 1124
source : BC7

86) chain A
residue 110
type
sequence I
description BINDING SITE FOR RESIDUE 78M A 1125
source : BC8

87) chain A
residue 117
type
sequence W
description BINDING SITE FOR RESIDUE 78M A 1125
source : BC8

88) chain D
residue 46
type
sequence A
description BINDING SITE FOR RESIDUE 78M A 1125
source : BC8

89) chain D
residue 47
type
sequence W
description BINDING SITE FOR RESIDUE 78M A 1125
source : BC8

90) chain D
residue 55
type
sequence R
description BINDING SITE FOR RESIDUE 78M A 1125
source : BC8

91) chain A
residue 41
type
sequence C
description BINDING SITE FOR RESIDUE 78M A 1126
source : BC9

92) chain A
residue 120
type
sequence F
description BINDING SITE FOR RESIDUE 78M A 1126
source : BC9

93) chain C
residue 102
type
sequence L
description BINDING SITE FOR RESIDUE 78M A 1126
source : BC9

94) chain C
residue 105
type
sequence I
description BINDING SITE FOR RESIDUE 78M A 1126
source : BC9

95) chain D
residue 39
type
sequence L
description BINDING SITE FOR RESIDUE 78M A 1126
source : BC9

96) chain A
residue 69-80
type prosite
sequence ELLNSAIEAVVD
description DAGK_PROKAR Prokaryotic diacylglycerol kinase signature. ElLNSAIEavVD
source prosite : PS01069

97) chain A
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

98) chain B
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

99) chain C
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

100) chain C
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

101) chain C
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

102) chain D
residue 16
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

103) chain D
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

104) chain D
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

105) chain D
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

106) chain A
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

107) chain D
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

108) chain E
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

109) chain E
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

110) chain E
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

111) chain F
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

112) chain F
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

113) chain A
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

114) chain F
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

115) chain A
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

116) chain A
residue 94
type BINDING
sequence K
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

117) chain B
residue 28
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

118) chain B
residue 76
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

119) chain B
residue 85
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:26673816, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI10

120) chain A
residue 22
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI11

121) chain D
residue 22
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI11

122) chain A
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

123) chain B
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

124) chain D
residue 30
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI12

125) chain A
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

126) chain B
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

127) chain C
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

128) chain D
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

129) chain F
residue 47
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI13

130) chain A
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

131) chain B
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

132) chain C
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

133) chain D
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

134) chain E
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

135) chain F
residue 55
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.25
source Swiss-Prot : SWS_FT_FI14

136) chain A
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

137) chain B
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

138) chain C
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

139) chain D
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

140) chain E
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

141) chain F
residue 69
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI15

142) chain A
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

143) chain B
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

144) chain C
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

145) chain D
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

146) chain E
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

147) chain F
residue 98
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI16

148) chain A
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

149) chain B
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

150) chain C
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

151) chain D
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

152) chain E
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

153) chain F
residue 112
type BINDING
sequence W
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:25055873, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129, ECO:0000305|Ref.26
source Swiss-Prot : SWS_FT_FI17

154) chain A
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLCVVIAAW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

155) chain E
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

156) chain F
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

157) chain A
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

158) chain B
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLCVVIAAW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

159) chain B
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

160) chain C
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

161) chain D
residue 31-47
type TRANSMEM
sequence FRQEGVAVLLCVVIAAW
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

162) chain D
residue 51-68
type TRANSMEM
sequence DAVTRVLLISSVMLVMIV
description Helical => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI2

163) chain A
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

164) chain B
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

165) chain C
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

166) chain D
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

167) chain F
residue 48-50
type TOPO_DOM
sequence LDV
description Periplasmic => ECO:0000305|PubMed:12379131, ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI3

168) chain A
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

169) chain B
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

170) chain C
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

171) chain D
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

172) chain E
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

173) chain F
residue 69-94
type TOPO_DOM
sequence ELLNSAIEAVVDRIGSEYHELSGRAK
description Cytoplasmic => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI4

174) chain A
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

175) chain B
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

176) chain C
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

177) chain D
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

178) chain E
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

179) chain F
residue 95-118
type TRANSMEM
sequence DLGSAAVLIAIIDAVITWAILLWS
description Helical => ECO:0000305|PubMed:8071224
source Swiss-Prot : SWS_FT_FI5

180) chain A
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

181) chain B
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

182) chain C
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

183) chain D
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

184) chain E
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

185) chain F
residue 119-121
type TOPO_DOM
sequence HFG
description Periplasmic => ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:8071224
source Swiss-Prot : SWS_FT_FI6

186) chain A
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

187) chain B
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

188) chain C
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

189) chain D
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

190) chain E
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

191) chain F
residue 69
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:26673816
source Swiss-Prot : SWS_FT_FI7

192) chain A
residue 9
type BINDING
sequence R
description BINDING => ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26673816, ECO:0000305|PubMed:26894538
source Swiss-Prot : SWS_FT_FI8

193) chain A
residue 13
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:23676677, ECO:0000305|PubMed:25012698, ECO:0000305|PubMed:26894538, ECO:0000305|PubMed:26960129
source Swiss-Prot : SWS_FT_FI9


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