eF-site ID 5irx-ABCDEF
PDB Code 5irx
Chain A, B, C, D, E, F

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Title Structure of TRPV1 in complex with DkTx and RTX, determined in lipid nanodisc
Classification TRANSPORT PROTEIN
Compound Transient receptor potential cation channel subfamily V member 1
Source (DKTX_HAPSC)
Sequence A:  TPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAY
GPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLL
VEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYY
RPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQ
YFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQR
KEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMIL
RDLCRFMFVYLVFLFGFSTAVVTLIEDGKYNSLYSTCLEL
FKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNM
LIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMR
KAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTT
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:  DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPV
TTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYR
F:  DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPV
TTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYR
Description (1)  Transient receptor potential cation channel subfamily V member 1, Tau-theraphotoxin-Hs1a


Functional site

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

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

3) chain A
residue 487
type
sequence Y
description binding site for residue 6O8 A 801
source : AC1

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

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

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

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

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

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

10) chain A
residue 629
type
sequence S
description binding site for residue 6OE A 802
source : AC2

11) chain A
residue 631
type
sequence Y
description binding site for residue 6OE A 802
source : AC2

12) chain C
residue 453
type
sequence Y
description binding site for residue 6OE A 802
source : AC2

13) chain F
residue 66
type
sequence A
description binding site for residue 6OE A 802
source : AC2

14) chain F
residue 67
type
sequence F
description binding site for residue 6OE A 802
source : AC2

15) chain A
residue 532
type
sequence S
description binding site for residue 6OE A 803
source : AC3

16) chain A
residue 534
type
sequence R
description binding site for residue 6OE A 803
source : AC3

17) chain A
residue 511
type
sequence Y
description binding site for residue 6EU A 804
source : AC4

18) chain A
residue 512
type
sequence S
description binding site for residue 6EU A 804
source : AC4

19) chain A
residue 514
type
sequence I
description binding site for residue 6EU A 804
source : AC4

20) chain A
residue 515
type
sequence L
description binding site for residue 6EU A 804
source : AC4

21) chain A
residue 546
type
sequence A
description binding site for residue 6EU A 804
source : AC4

22) chain A
residue 547
type
sequence M
description binding site for residue 6EU A 804
source : AC4

23) chain A
residue 550
type
sequence T
description binding site for residue 6EU A 804
source : AC4

24) chain A
residue 551
type
sequence N
description binding site for residue 6EU A 804
source : AC4

25) chain A
residue 553
type
sequence L
description binding site for residue 6EU A 804
source : AC4

26) chain A
residue 554
type
sequence Y
description binding site for residue 6EU A 804
source : AC4

27) chain A
residue 557
type
sequence R
description binding site for residue 6EU A 804
source : AC4

28) chain A
residue 566
type
sequence A
description binding site for residue 6EU A 804
source : AC4

29) chain A
residue 569
type
sequence I
description binding site for residue 6EU A 804
source : AC4

30) chain A
residue 573
type
sequence I
description binding site for residue 6EU A 804
source : AC4

31) chain B
residue 591
type
sequence F
description binding site for residue 6EU A 804
source : AC4

32) chain B
residue 668
type
sequence I
description binding site for residue 6EU A 804
source : AC4

33) chain B
residue 669
type
sequence L
description binding site for residue 6EU A 804
source : AC4

34) chain B
residue 437
type
sequence N
description binding site for residue 6O8 B 801
source : AC5

35) chain B
residue 440
type
sequence V
description binding site for residue 6O8 B 801
source : AC5

36) chain B
residue 487
type
sequence Y
description binding site for residue 6O8 B 801
source : AC5

37) chain B
residue 488
type
sequence F
description binding site for residue 6O8 B 801
source : AC5

38) chain B
residue 491
type
sequence R
description binding site for residue 6O8 B 801
source : AC5

39) chain B
residue 513
type
sequence E
description binding site for residue 6O8 B 801
source : AC5

40) chain B
residue 516
type
sequence F
description binding site for residue 6O8 B 801
source : AC5

41) chain B
residue 554
type
sequence Y
description binding site for residue 6O8 B 801
source : AC5

42) chain B
residue 555
type
sequence Y
description binding site for residue 6O8 B 801
source : AC5

43) chain B
residue 532
type
sequence S
description binding site for residue 6OE B 802
source : AC6

44) chain B
residue 534
type
sequence R
description binding site for residue 6OE B 802
source : AC6

45) chain B
residue 511
type
sequence Y
description binding site for residue 6EU B 803
source : AC7

46) chain B
residue 512
type
sequence S
description binding site for residue 6EU B 803
source : AC7

47) chain B
residue 514
type
sequence I
description binding site for residue 6EU B 803
source : AC7

48) chain B
residue 515
type
sequence L
description binding site for residue 6EU B 803
source : AC7

49) chain B
residue 546
type
sequence A
description binding site for residue 6EU B 803
source : AC7

50) chain B
residue 547
type
sequence M
description binding site for residue 6EU B 803
source : AC7

51) chain B
residue 550
type
sequence T
description binding site for residue 6EU B 803
source : AC7

52) chain B
residue 551
type
sequence N
description binding site for residue 6EU B 803
source : AC7

53) chain B
residue 553
type
sequence L
description binding site for residue 6EU B 803
source : AC7

54) chain B
residue 554
type
sequence Y
description binding site for residue 6EU B 803
source : AC7

55) chain B
residue 557
type
sequence R
description binding site for residue 6EU B 803
source : AC7

56) chain B
residue 566
type
sequence A
description binding site for residue 6EU B 803
source : AC7

57) chain B
residue 569
type
sequence I
description binding site for residue 6EU B 803
source : AC7

58) chain B
residue 573
type
sequence I
description binding site for residue 6EU B 803
source : AC7

59) chain D
residue 591
type
sequence F
description binding site for residue 6EU B 803
source : AC7

60) chain D
residue 668
type
sequence I
description binding site for residue 6EU B 803
source : AC7

61) chain D
residue 669
type
sequence L
description binding site for residue 6EU B 803
source : AC7

62) chain C
residue 437
type
sequence N
description binding site for residue 6O8 C 801
source : AC8

63) chain C
residue 440
type
sequence V
description binding site for residue 6O8 C 801
source : AC8

64) chain C
residue 487
type
sequence Y
description binding site for residue 6O8 C 801
source : AC8

65) chain C
residue 488
type
sequence F
description binding site for residue 6O8 C 801
source : AC8

66) chain C
residue 491
type
sequence R
description binding site for residue 6O8 C 801
source : AC8

67) chain C
residue 513
type
sequence E
description binding site for residue 6O8 C 801
source : AC8

68) chain C
residue 516
type
sequence F
description binding site for residue 6O8 C 801
source : AC8

69) chain C
residue 554
type
sequence Y
description binding site for residue 6O8 C 801
source : AC8

70) chain C
residue 555
type
sequence Y
description binding site for residue 6O8 C 801
source : AC8

71) chain C
residue 534
type
sequence R
description binding site for residue 6OE C 802
source : AC9

72) chain A
residue 591
type
sequence F
description binding site for residue 6EU C 803
source : AD1

73) chain A
residue 668
type
sequence I
description binding site for residue 6EU C 803
source : AD1

74) chain A
residue 669
type
sequence L
description binding site for residue 6EU C 803
source : AD1

75) chain C
residue 511
type
sequence Y
description binding site for residue 6EU C 803
source : AD1

76) chain C
residue 512
type
sequence S
description binding site for residue 6EU C 803
source : AD1

77) chain C
residue 514
type
sequence I
description binding site for residue 6EU C 803
source : AD1

78) chain C
residue 515
type
sequence L
description binding site for residue 6EU C 803
source : AD1

79) chain C
residue 546
type
sequence A
description binding site for residue 6EU C 803
source : AD1

80) chain C
residue 547
type
sequence M
description binding site for residue 6EU C 803
source : AD1

81) chain C
residue 550
type
sequence T
description binding site for residue 6EU C 803
source : AD1

82) chain C
residue 551
type
sequence N
description binding site for residue 6EU C 803
source : AD1

83) chain C
residue 553
type
sequence L
description binding site for residue 6EU C 803
source : AD1

84) chain C
residue 554
type
sequence Y
description binding site for residue 6EU C 803
source : AD1

85) chain C
residue 557
type
sequence R
description binding site for residue 6EU C 803
source : AD1

86) chain C
residue 566
type
sequence A
description binding site for residue 6EU C 803
source : AD1

87) chain C
residue 569
type
sequence I
description binding site for residue 6EU C 803
source : AD1

88) chain C
residue 573
type
sequence I
description binding site for residue 6EU C 803
source : AD1

89) chain D
residue 437
type
sequence N
description binding site for residue 6O8 D 801
source : AD2

90) chain D
residue 440
type
sequence V
description binding site for residue 6O8 D 801
source : AD2

91) chain D
residue 487
type
sequence Y
description binding site for residue 6O8 D 801
source : AD2

92) chain D
residue 488
type
sequence F
description binding site for residue 6O8 D 801
source : AD2

93) chain D
residue 491
type
sequence R
description binding site for residue 6O8 D 801
source : AD2

94) chain D
residue 513
type
sequence E
description binding site for residue 6O8 D 801
source : AD2

95) chain D
residue 516
type
sequence F
description binding site for residue 6O8 D 801
source : AD2

96) chain D
residue 554
type
sequence Y
description binding site for residue 6O8 D 801
source : AD2

97) chain D
residue 555
type
sequence Y
description binding site for residue 6O8 D 801
source : AD2

98) chain D
residue 534
type
sequence R
description binding site for residue 6O9 D 802
source : AD3

99) chain E
residue 50
type
sequence V
description binding site for residue 6O9 D 802
source : AD3

100) chain E
residue 53
type
sequence W
description binding site for residue 6O9 D 802
source : AD3

101) chain B
residue 453
type
sequence Y
description binding site for residue 6OE D 803
source : AD4

102) chain D
residue 629
type
sequence S
description binding site for residue 6OE D 803
source : AD4

103) chain D
residue 631
type
sequence Y
description binding site for residue 6OE D 803
source : AD4

104) chain E
residue 66
type
sequence A
description binding site for residue 6OE D 803
source : AD4

105) chain E
residue 67
type
sequence F
description binding site for residue 6OE D 803
source : AD4

106) chain D
residue 532
type
sequence S
description binding site for residue 6OE D 804
source : AD5

107) chain D
residue 534
type
sequence R
description binding site for residue 6OE D 804
source : AD5

108) chain C
residue 591
type
sequence F
description binding site for residue 6EU D 805
source : AD6

109) chain C
residue 668
type
sequence I
description binding site for residue 6EU D 805
source : AD6

110) chain C
residue 669
type
sequence L
description binding site for residue 6EU D 805
source : AD6

111) chain D
residue 511
type
sequence Y
description binding site for residue 6EU D 805
source : AD6

112) chain D
residue 512
type
sequence S
description binding site for residue 6EU D 805
source : AD6

113) chain D
residue 514
type
sequence I
description binding site for residue 6EU D 805
source : AD6

114) chain D
residue 515
type
sequence L
description binding site for residue 6EU D 805
source : AD6

115) chain D
residue 546
type
sequence A
description binding site for residue 6EU D 805
source : AD6

116) chain D
residue 547
type
sequence M
description binding site for residue 6EU D 805
source : AD6

117) chain D
residue 550
type
sequence T
description binding site for residue 6EU D 805
source : AD6

118) chain D
residue 551
type
sequence N
description binding site for residue 6EU D 805
source : AD6

119) chain D
residue 553
type
sequence L
description binding site for residue 6EU D 805
source : AD6

120) chain D
residue 554
type
sequence Y
description binding site for residue 6EU D 805
source : AD6

121) chain D
residue 557
type
sequence R
description binding site for residue 6EU D 805
source : AD6

122) chain D
residue 566
type
sequence A
description binding site for residue 6EU D 805
source : AD6

123) chain D
residue 569
type
sequence I
description binding site for residue 6EU D 805
source : AD6

124) chain D
residue 573
type
sequence I
description binding site for residue 6EU D 805
source : AD6

125) chain C
residue 534
type
sequence R
description binding site for residue 6O9 E 101
source : AD7

126) chain E
residue 7
type
sequence E
description binding site for residue 6O9 E 101
source : AD7

127) chain E
residue 8
type
sequence V
description binding site for residue 6O9 E 101
source : AD7

128) chain E
residue 11
type
sequence W
description binding site for residue 6O9 E 101
source : AD7

129) chain C
residue 629
type
sequence S
description binding site for residue 6OE E 102
source : AD8

130) chain C
residue 631
type
sequence Y
description binding site for residue 6OE E 102
source : AD8

131) chain D
residue 453
type
sequence Y
description binding site for residue 6OE E 102
source : AD8

132) chain E
residue 26
type
sequence E
description binding site for residue 6OE E 102
source : AD8

133) chain B
residue 534
type
sequence R
description binding site for residue 6O9 F 101
source : AD9

134) chain F
residue 7
type
sequence E
description binding site for residue 6O9 F 101
source : AD9

135) chain F
residue 8
type
sequence V
description binding site for residue 6O9 F 101
source : AD9

136) chain A
residue 534
type
sequence R
description binding site for residue 6O9 F 102
source : AE1

137) chain F
residue 49
type
sequence E
description binding site for residue 6O9 F 102
source : AE1

138) chain F
residue 50
type
sequence V
description binding site for residue 6O9 F 102
source : AE1

139) chain A
residue 453
type
sequence Y
description binding site for residue 6OE F 103
source : AE2

140) chain B
residue 629
type
sequence S
description binding site for residue 6OE F 103
source : AE2

141) chain B
residue 631
type
sequence Y
description binding site for residue 6OE F 103
source : AE2

142) chain F
residue 26
type
sequence E
description binding site for residue 6OE F 103
source : AE2

143) chain A
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

144) chain B
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

145) 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

146) chain D
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

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

148) 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

149) 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

150) 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

151) chain A
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

152) 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

153) 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

154) 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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

180) 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

181) 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

182) 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

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

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

185) 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

186) 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

187) 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

188) 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

189) 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

190) 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

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

192) 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

193) 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

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

195) 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

196) 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

197) 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

198) 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

199) 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

200) 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

201) 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

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

203) 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

204) 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

205) 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

206) 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

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

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

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

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

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

212) 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

213) 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

214) 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

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

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

217) 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

218) 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

219) 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

220) 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

221) 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

222) 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


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