eF-site ID 5irz-BCDE
PDB Code 5irz
Chain B, C, D, E

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Title Structure of TRPV1 determined in lipid nanodisc
Classification TRANSPORT PROTEIN
Compound Transient receptor potential cation channel subfamily V member 1
Source (TRPV1_RAT)
Sequence B:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
C:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
D:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
E:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
Description


Functional site

1) chain D
residue 437
type
sequence N
description binding site for residue 6O8 D 801
source : AC1

2) chain D
residue 440
type
sequence V
description binding site for residue 6O8 D 801
source : AC1

3) chain D
residue 488
type
sequence F
description binding site for residue 6O8 D 801
source : AC1

4) chain D
residue 491
type
sequence R
description binding site for residue 6O8 D 801
source : AC1

5) chain D
residue 513
type
sequence E
description binding site for residue 6O8 D 801
source : AC1

6) chain D
residue 516
type
sequence F
description binding site for residue 6O8 D 801
source : AC1

7) chain D
residue 554
type
sequence Y
description binding site for residue 6O8 D 801
source : AC1

8) chain D
residue 555
type
sequence Y
description binding site for residue 6O8 D 801
source : AC1

9) chain D
residue 509
type
sequence D
description binding site for residue 6ES D 802
source : AC2

10) chain D
residue 510
type
sequence S
description binding site for residue 6ES D 802
source : AC2

11) chain D
residue 511
type
sequence Y
description binding site for residue 6ES D 802
source : AC2

12) chain D
residue 512
type
sequence S
description binding site for residue 6ES D 802
source : AC2

13) chain D
residue 550
type
sequence T
description binding site for residue 6ES D 802
source : AC2

14) chain D
residue 557
type
sequence R
description binding site for residue 6ES D 802
source : AC2

15) chain D
residue 570
type
sequence E
description binding site for residue 6ES D 802
source : AC2

16) chain D
residue 699
type
sequence L
description binding site for residue 6ES D 802
source : AC2

17) chain D
residue 700
type
sequence Q
description binding site for residue 6ES D 802
source : AC2

18) chain D
residue 631
type
sequence Y
description binding site for residue 6OE D 803
source : AC3

19) chain E
residue 657
type
sequence A
description binding site for residue 6OE D 803
source : AC3

20) chain D
residue 655
type
sequence F
description binding site for residue 6OE D 804
source : AC4

21) chain D
residue 453
type
sequence Y
description binding site for residue 6OE D 805
source : AC5

22) chain D
residue 454
type
sequence Y
description binding site for residue 6OE D 805
source : AC5

23) chain E
residue 589
type
sequence F
description binding site for residue 6OE D 805
source : AC5

24) chain E
residue 629
type
sequence S
description binding site for residue 6OE D 805
source : AC5

25) chain D
residue 454
type
sequence Y
description binding site for residue 6OE D 806
source : AC6

26) chain D
residue 470
type
sequence G
description binding site for residue 6OE D 806
source : AC6

27) chain D
residue 473
type
sequence F
description binding site for residue 6OE D 806
source : AC6

28) chain D
residue 474
type
sequence R
description binding site for residue 6OE D 806
source : AC6

29) chain E
residue 437
type
sequence N
description binding site for residue 6O8 E 801
source : AC7

30) chain E
residue 440
type
sequence V
description binding site for residue 6O8 E 801
source : AC7

31) chain E
residue 488
type
sequence F
description binding site for residue 6O8 E 801
source : AC7

32) chain E
residue 491
type
sequence R
description binding site for residue 6O8 E 801
source : AC7

33) chain E
residue 513
type
sequence E
description binding site for residue 6O8 E 801
source : AC7

34) chain E
residue 516
type
sequence F
description binding site for residue 6O8 E 801
source : AC7

35) chain E
residue 554
type
sequence Y
description binding site for residue 6O8 E 801
source : AC7

36) chain E
residue 555
type
sequence Y
description binding site for residue 6O8 E 801
source : AC7

37) chain E
residue 509
type
sequence D
description binding site for residue 6ES E 802
source : AC8

38) chain E
residue 510
type
sequence S
description binding site for residue 6ES E 802
source : AC8

39) chain E
residue 511
type
sequence Y
description binding site for residue 6ES E 802
source : AC8

40) chain E
residue 512
type
sequence S
description binding site for residue 6ES E 802
source : AC8

41) chain E
residue 550
type
sequence T
description binding site for residue 6ES E 802
source : AC8

42) chain E
residue 557
type
sequence R
description binding site for residue 6ES E 802
source : AC8

43) chain E
residue 570
type
sequence E
description binding site for residue 6ES E 802
source : AC8

44) chain E
residue 699
type
sequence L
description binding site for residue 6ES E 802
source : AC8

45) chain E
residue 700
type
sequence Q
description binding site for residue 6ES E 802
source : AC8

46) chain E
residue 655
type
sequence F
description binding site for residue 6OE E 803
source : AC9

47) chain C
residue 589
type
sequence F
description binding site for residue 6OE E 804
source : AD1

48) chain C
residue 629
type
sequence S
description binding site for residue 6OE E 804
source : AD1

49) chain E
residue 453
type
sequence Y
description binding site for residue 6OE E 804
source : AD1

50) chain E
residue 454
type
sequence Y
description binding site for residue 6OE E 804
source : AD1

51) chain E
residue 454
type
sequence Y
description binding site for residue 6OE E 805
source : AD2

52) chain E
residue 470
type
sequence G
description binding site for residue 6OE E 805
source : AD2

53) chain E
residue 473
type
sequence F
description binding site for residue 6OE E 805
source : AD2

54) chain E
residue 474
type
sequence R
description binding site for residue 6OE E 805
source : AD2

55) chain C
residue 657
type
sequence A
description binding site for residue 6OE E 806
source : AD3

56) chain E
residue 631
type
sequence Y
description binding site for residue 6OE E 806
source : AD3

57) chain B
residue 509
type
sequence D
description binding site for residue 6ES B 802
source : AD4

58) chain B
residue 510
type
sequence S
description binding site for residue 6ES B 802
source : AD4

59) chain B
residue 511
type
sequence Y
description binding site for residue 6ES B 802
source : AD4

60) chain B
residue 512
type
sequence S
description binding site for residue 6ES B 802
source : AD4

61) chain B
residue 550
type
sequence T
description binding site for residue 6ES B 802
source : AD4

62) chain B
residue 557
type
sequence R
description binding site for residue 6ES B 802
source : AD4

63) chain B
residue 570
type
sequence E
description binding site for residue 6ES B 802
source : AD4

64) chain B
residue 699
type
sequence L
description binding site for residue 6ES B 802
source : AD4

65) chain B
residue 700
type
sequence Q
description binding site for residue 6ES B 802
source : AD4

66) chain B
residue 453
type
sequence Y
description binding site for residue 6OE B 803
source : AD5

67) chain B
residue 454
type
sequence Y
description binding site for residue 6OE B 803
source : AD5

68) chain D
residue 589
type
sequence F
description binding site for residue 6OE B 803
source : AD5

69) chain D
residue 629
type
sequence S
description binding site for residue 6OE B 803
source : AD5

70) chain B
residue 454
type
sequence Y
description binding site for residue 6OE B 804
source : AD6

71) chain B
residue 470
type
sequence G
description binding site for residue 6OE B 804
source : AD6

72) chain B
residue 473
type
sequence F
description binding site for residue 6OE B 804
source : AD6

73) chain B
residue 474
type
sequence R
description binding site for residue 6OE B 804
source : AD6

74) chain B
residue 631
type
sequence Y
description binding site for residue 6OE B 805
source : AD7

75) chain D
residue 657
type
sequence A
description binding site for residue 6OE B 805
source : AD7

76) chain B
residue 655
type
sequence F
description binding site for residue 6OE B 806
source : AD8

77) chain C
residue 509
type
sequence D
description binding site for residue 6ES C 802
source : AD9

78) chain C
residue 510
type
sequence S
description binding site for residue 6ES C 802
source : AD9

79) chain C
residue 511
type
sequence Y
description binding site for residue 6ES C 802
source : AD9

80) chain C
residue 512
type
sequence S
description binding site for residue 6ES C 802
source : AD9

81) chain C
residue 550
type
sequence T
description binding site for residue 6ES C 802
source : AD9

82) chain C
residue 557
type
sequence R
description binding site for residue 6ES C 802
source : AD9

83) chain C
residue 570
type
sequence E
description binding site for residue 6ES C 802
source : AD9

84) chain C
residue 699
type
sequence L
description binding site for residue 6ES C 802
source : AD9

85) chain C
residue 700
type
sequence Q
description binding site for residue 6ES C 802
source : AD9

86) chain B
residue 589
type
sequence F
description binding site for residue 6OE C 803
source : AE1

87) chain B
residue 629
type
sequence S
description binding site for residue 6OE C 803
source : AE1

88) chain C
residue 453
type
sequence Y
description binding site for residue 6OE C 803
source : AE1

89) chain C
residue 454
type
sequence Y
description binding site for residue 6OE C 803
source : AE1

90) chain C
residue 454
type
sequence Y
description binding site for residue 6OE C 804
source : AE2

91) chain C
residue 470
type
sequence G
description binding site for residue 6OE C 804
source : AE2

92) chain C
residue 473
type
sequence F
description binding site for residue 6OE C 804
source : AE2

93) chain C
residue 474
type
sequence R
description binding site for residue 6OE C 804
source : AE2

94) chain B
residue 657
type
sequence A
description binding site for residue 6OE C 805
source : AE3

95) chain C
residue 631
type
sequence Y
description binding site for residue 6OE C 805
source : AE3

96) chain C
residue 655
type
sequence F
description binding site for residue 6OE C 806
source : AE4

97) chain B
residue 437
type
sequence N
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

98) chain B
residue 440
type
sequence V
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

99) chain B
residue 487
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

100) chain B
residue 488
type
sequence F
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

101) chain B
residue 489
type
sequence F
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

102) chain B
residue 490
type
sequence F
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

103) chain B
residue 492
type
sequence G
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

104) chain B
residue 493
type
sequence I
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

105) chain B
residue 494
type
sequence Q
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

106) chain B
residue 495
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

107) chain B
residue 513
type
sequence E
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

108) chain B
residue 516
type
sequence F
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

109) chain B
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

110) chain B
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and ARG B 491
source : AE5

111) chain B
residue 437
type
sequence N
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

112) chain B
residue 440
type
sequence V
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

113) chain B
residue 488
type
sequence F
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

114) chain B
residue 491
type
sequence R
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

115) chain B
residue 512
type
sequence S
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

116) chain B
residue 513
type
sequence E
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

117) chain B
residue 514
type
sequence I
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

118) chain B
residue 515
type
sequence L
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

119) chain B
residue 517
type
sequence F
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

120) chain B
residue 518
type
sequence V
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

121) chain B
residue 520
type
sequence S
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

122) chain B
residue 551
type
sequence N
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

123) chain B
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

124) chain B
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 B 801 and PHE B 516
source : AE6

125) chain C
residue 437
type
sequence N
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

126) chain C
residue 440
type
sequence V
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

127) chain C
residue 488
type
sequence F
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

128) chain C
residue 491
type
sequence R
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

129) chain C
residue 512
type
sequence S
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

130) chain C
residue 513
type
sequence E
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

131) chain C
residue 514
type
sequence I
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

132) chain C
residue 515
type
sequence L
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

133) chain C
residue 517
type
sequence F
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

134) chain C
residue 518
type
sequence V
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

135) chain C
residue 520
type
sequence S
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

136) chain C
residue 551
type
sequence N
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

137) chain C
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

138) chain C
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and PHE C 516
source : AE7

139) chain C
residue 437
type
sequence N
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

140) chain C
residue 440
type
sequence V
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

141) chain C
residue 487
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

142) chain C
residue 488
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

143) chain C
residue 489
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

144) chain C
residue 490
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

145) chain C
residue 492
type
sequence G
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

146) chain C
residue 493
type
sequence I
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

147) chain C
residue 494
type
sequence Q
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

148) chain C
residue 495
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

149) chain C
residue 513
type
sequence E
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

150) chain C
residue 516
type
sequence F
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

151) chain C
residue 554
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

152) chain C
residue 555
type
sequence Y
description binding site for Di-peptide 6O8 C 801 and ARG C 491
source : AE8

153) chain D
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10

154) chain E
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10

155) chain B
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10

156) chain C
residue 370
type MOD_RES
sequence T
description Phosphothreonine; by PKA; in vitro => ECO:0000269|PubMed:12194871
source Swiss-Prot : SWS_FT_FI10

157) chain D
residue 502
type MOD_RES
sequence S
description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI11

158) chain E
residue 502
type MOD_RES
sequence S
description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI11

159) chain B
residue 502
type MOD_RES
sequence S
description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI11

160) chain C
residue 502
type MOD_RES
sequence S
description Phosphoserine; by PKC/PRKCE => ECO:0000269|PubMed:11884385, ECO:0000269|PubMed:12194871, ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI11

161) chain D
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

162) chain E
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

163) chain E
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

164) chain E
residue 681-709
type TRANSMEM
sequence LMGETVNKIAQESKNIWKLQRAITILDTE
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

165) chain B
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

166) chain B
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

167) chain B
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

168) chain B
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

169) chain B
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

170) chain B
residue 658-686
type TRANSMEM
sequence VFIILLLAYVILTYILLLNMLIALMGETV
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

171) chain C
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

172) chain D
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

173) chain C
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

174) chain C
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

175) chain C
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

176) chain C
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

177) chain C
residue 658-686
type TRANSMEM
sequence VFIILLLAYVILTYILLLNMLIALMGETV
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

178) chain D
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

179) chain D
residue 536-556
type TRANSMEM
sequence EYVASMVFSLAMGWTNMLYYT
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

180) chain D
residue 572-599
type TRANSMEM
sequence MILRDLCRFMFVYLVFLFGFSTAVVTLI
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

181) chain D
residue 658-686
type TRANSMEM
sequence VFIILLLAYVILTYILLLNMLIALMGETV
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

182) chain E
residue 433-453
type TRANSMEM
sequence IFYFNFFVYCLYMIIFTAAAY
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

183) chain E
residue 472-497
type TRANSMEM
sequence YFRVTGEILSVSGGVYFFFRGIQYFL
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

184) chain E
residue 511-531
type TRANSMEM
sequence YSEILFFVQSLFMLVSVVLYF
description Helical => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI1

185) chain D
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

186) chain E
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

187) chain B
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

188) chain C
residue 627
type CARBOHYD
sequence Y
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11683872
source Swiss-Prot : SWS_FT_FI13

189) chain D
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

190) chain C
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

191) chain C
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

192) chain C
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

193) chain D
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

194) chain D
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

195) chain E
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

196) chain E
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

197) chain E
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

198) chain B
residue 454-471
type TOPO_DOM
sequence YRPVEGLPPYKLKNTVGD
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

199) chain B
residue 532-535
type TOPO_DOM
sequence SQRK
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

200) chain B
residue 600-649
type TOPO_DOM
sequence EDGKYNSLYSTCLELFKFTIGMGDLEF
description Extracellular => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI2

201) chain D
residue 498-510
type TOPO_DOM
sequence QRRPSLKSLFVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

202) chain D
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

203) chain E
residue 498-510
type TOPO_DOM
sequence QRRPSLKSLFVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

204) chain E
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

205) chain B
residue 498-510
type TOPO_DOM
sequence QRRPSLKSLFVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

206) chain B
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

207) chain C
residue 498-510
type TOPO_DOM
sequence QRRPSLKSLFVDS
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

208) chain C
residue 557-571
type TOPO_DOM
sequence RGFQQMGIYAVMIEK
description Cytoplasmic => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200
source Swiss-Prot : SWS_FT_FI3

209) chain D
residue 627-649
type INTRAMEM
sequence YNSLYSTCLELFKFTIGMGDLEF
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4

210) chain E
residue 650-672
type INTRAMEM
sequence TENYDFKAVFIILLLAYVILTYI
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4

211) chain B
residue 627-649
type INTRAMEM
sequence YNSLYSTCLELFKFTIGMGDLEF
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4

212) chain C
residue 627-649
type INTRAMEM
sequence YNSLYSTCLELFKFTIGMGDLEF
description Pore-forming => ECO:0000269|PubMed:24305160, ECO:0000269|PubMed:27281200, ECO:0000305|PubMed:10931826
source Swiss-Prot : SWS_FT_FI4

213) chain D
residue 704
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12

214) chain E
residue 727
type MOD_RES
sequence Q
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12

215) chain B
residue 704
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12

216) chain C
residue 704
type MOD_RES
sequence T
description Phosphothreonine => ECO:0000269|PubMed:14630912
source Swiss-Prot : SWS_FT_FI12

217) chain D
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

218) chain C
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

219) chain C
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

220) chain C
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

221) chain D
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

222) chain D
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

223) chain E
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

224) chain E
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

225) chain E
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

226) chain B
residue 511
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

227) chain B
residue 550
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

228) chain B
residue 557
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:27281200, ECO:0007744|PDB:5IRX
source Swiss-Prot : SWS_FT_FI7

229) chain D
residue 646
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8

230) chain E
residue 669
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8

231) chain B
residue 646
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8

232) chain C
residue 646
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q9R186
source Swiss-Prot : SWS_FT_FI8


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