eF-site ID 5q08-ABCDEFGH
PDB Code 5q08
Chain A, B, C, D, E, F, G, H

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Title Human liver fructose-1,6-bisphosphatase 1 (fructose 1,6-bisphosphate 1-phosphatase, E.C.3.1.3.11) complexed with the allosteric inhibitor 1-(1-benzothiophen-3-ylsulfonyl)-3-(5-bromo-1,3-thiazol-2-yl)urea
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Fructose-1,6-bisphosphatase 1
Source (Q2TU34_HUMAN)
Sequence A:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS
EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF
GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA
MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT
TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
B:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
C:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS
EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF
GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA
MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT
TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
E:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGVKKLDVLSNDLVMNMLKSSFATCVLVS
EEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIF
GIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLA
MDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYA
KDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTL
VYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMAT
TGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
F:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
G:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
H:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain A
residue 17
type
sequence V
description binding site for residue 967 A 401
source : AC1

2) chain A
residue 18
type
sequence M
description binding site for residue 967 A 401
source : AC1

3) chain A
residue 21
type
sequence G
description binding site for residue 967 A 401
source : AC1

4) chain A
residue 22
type
sequence R
description binding site for residue 967 A 401
source : AC1

5) chain A
residue 24
type
sequence A
description binding site for residue 967 A 401
source : AC1

6) chain A
residue 26
type
sequence G
description binding site for residue 967 A 401
source : AC1

7) chain A
residue 27
type
sequence T
description binding site for residue 967 A 401
source : AC1

8) chain A
residue 28
type
sequence G
description binding site for residue 967 A 401
source : AC1

9) chain A
residue 29
type
sequence E
description binding site for residue 967 A 401
source : AC1

10) chain A
residue 30
type
sequence L
description binding site for residue 967 A 401
source : AC1

11) chain A
residue 31
type
sequence T
description binding site for residue 967 A 401
source : AC1

12) chain C
residue 27
type
sequence T
description binding site for residue 967 A 401
source : AC1

13) chain B
residue 17
type
sequence V
description binding site for residue 967 B 401
source : AC2

14) chain B
residue 21
type
sequence G
description binding site for residue 967 B 401
source : AC2

15) chain B
residue 22
type
sequence R
description binding site for residue 967 B 401
source : AC2

16) chain B
residue 24
type
sequence A
description binding site for residue 967 B 401
source : AC2

17) chain B
residue 26
type
sequence G
description binding site for residue 967 B 401
source : AC2

18) chain B
residue 27
type
sequence T
description binding site for residue 967 B 401
source : AC2

19) chain B
residue 28
type
sequence G
description binding site for residue 967 B 401
source : AC2

20) chain B
residue 29
type
sequence E
description binding site for residue 967 B 401
source : AC2

21) chain B
residue 30
type
sequence L
description binding site for residue 967 B 401
source : AC2

22) chain B
residue 31
type
sequence T
description binding site for residue 967 B 401
source : AC2

23) chain D
residue 27
type
sequence T
description binding site for residue 967 B 401
source : AC2

24) chain D
residue 28
type
sequence G
description binding site for residue 967 B 401
source : AC2

25) chain A
residue 27
type
sequence T
description binding site for residue 967 C 401
source : AC3

26) chain A
residue 28
type
sequence G
description binding site for residue 967 C 401
source : AC3

27) chain C
residue 17
type
sequence V
description binding site for residue 967 C 401
source : AC3

28) chain C
residue 18
type
sequence M
description binding site for residue 967 C 401
source : AC3

29) chain C
residue 21
type
sequence G
description binding site for residue 967 C 401
source : AC3

30) chain C
residue 22
type
sequence R
description binding site for residue 967 C 401
source : AC3

31) chain C
residue 24
type
sequence A
description binding site for residue 967 C 401
source : AC3

32) chain C
residue 26
type
sequence G
description binding site for residue 967 C 401
source : AC3

33) chain C
residue 27
type
sequence T
description binding site for residue 967 C 401
source : AC3

34) chain C
residue 28
type
sequence G
description binding site for residue 967 C 401
source : AC3

35) chain C
residue 29
type
sequence E
description binding site for residue 967 C 401
source : AC3

36) chain C
residue 30
type
sequence L
description binding site for residue 967 C 401
source : AC3

37) chain C
residue 31
type
sequence T
description binding site for residue 967 C 401
source : AC3

38) chain B
residue 27
type
sequence T
description binding site for residue 967 D 401
source : AC4

39) chain B
residue 28
type
sequence G
description binding site for residue 967 D 401
source : AC4

40) chain D
residue 17
type
sequence V
description binding site for residue 967 D 401
source : AC4

41) chain D
residue 21
type
sequence G
description binding site for residue 967 D 401
source : AC4

42) chain D
residue 22
type
sequence R
description binding site for residue 967 D 401
source : AC4

43) chain D
residue 24
type
sequence A
description binding site for residue 967 D 401
source : AC4

44) chain D
residue 26
type
sequence G
description binding site for residue 967 D 401
source : AC4

45) chain D
residue 27
type
sequence T
description binding site for residue 967 D 401
source : AC4

46) chain D
residue 28
type
sequence G
description binding site for residue 967 D 401
source : AC4

47) chain D
residue 29
type
sequence E
description binding site for residue 967 D 401
source : AC4

48) chain D
residue 30
type
sequence L
description binding site for residue 967 D 401
source : AC4

49) chain D
residue 31
type
sequence T
description binding site for residue 967 D 401
source : AC4

50) chain E
residue 17
type
sequence V
description binding site for residue 967 E 401
source : AC5

51) chain E
residue 21
type
sequence G
description binding site for residue 967 E 401
source : AC5

52) chain E
residue 22
type
sequence R
description binding site for residue 967 E 401
source : AC5

53) chain E
residue 24
type
sequence A
description binding site for residue 967 E 401
source : AC5

54) chain E
residue 26
type
sequence G
description binding site for residue 967 E 401
source : AC5

55) chain E
residue 27
type
sequence T
description binding site for residue 967 E 401
source : AC5

56) chain E
residue 28
type
sequence G
description binding site for residue 967 E 401
source : AC5

57) chain E
residue 29
type
sequence E
description binding site for residue 967 E 401
source : AC5

58) chain E
residue 30
type
sequence L
description binding site for residue 967 E 401
source : AC5

59) chain E
residue 31
type
sequence T
description binding site for residue 967 E 401
source : AC5

60) chain G
residue 27
type
sequence T
description binding site for residue 967 E 401
source : AC5

61) chain G
residue 28
type
sequence G
description binding site for residue 967 E 401
source : AC5

62) chain F
residue 17
type
sequence V
description binding site for residue 967 F 401
source : AC6

63) chain F
residue 18
type
sequence M
description binding site for residue 967 F 401
source : AC6

64) chain F
residue 21
type
sequence G
description binding site for residue 967 F 401
source : AC6

65) chain F
residue 22
type
sequence R
description binding site for residue 967 F 401
source : AC6

66) chain F
residue 24
type
sequence A
description binding site for residue 967 F 401
source : AC6

67) chain F
residue 26
type
sequence G
description binding site for residue 967 F 401
source : AC6

68) chain F
residue 27
type
sequence T
description binding site for residue 967 F 401
source : AC6

69) chain F
residue 28
type
sequence G
description binding site for residue 967 F 401
source : AC6

70) chain F
residue 29
type
sequence E
description binding site for residue 967 F 401
source : AC6

71) chain F
residue 30
type
sequence L
description binding site for residue 967 F 401
source : AC6

72) chain F
residue 31
type
sequence T
description binding site for residue 967 F 401
source : AC6

73) chain H
residue 27
type
sequence T
description binding site for residue 967 F 401
source : AC6

74) chain H
residue 28
type
sequence G
description binding site for residue 967 F 401
source : AC6

75) chain E
residue 27
type
sequence T
description binding site for residue 967 G 401
source : AC7

76) chain E
residue 28
type
sequence G
description binding site for residue 967 G 401
source : AC7

77) chain G
residue 17
type
sequence V
description binding site for residue 967 G 401
source : AC7

78) chain G
residue 18
type
sequence M
description binding site for residue 967 G 401
source : AC7

79) chain G
residue 21
type
sequence G
description binding site for residue 967 G 401
source : AC7

80) chain G
residue 22
type
sequence R
description binding site for residue 967 G 401
source : AC7

81) chain G
residue 24
type
sequence A
description binding site for residue 967 G 401
source : AC7

82) chain G
residue 26
type
sequence G
description binding site for residue 967 G 401
source : AC7

83) chain G
residue 27
type
sequence T
description binding site for residue 967 G 401
source : AC7

84) chain G
residue 28
type
sequence G
description binding site for residue 967 G 401
source : AC7

85) chain G
residue 29
type
sequence E
description binding site for residue 967 G 401
source : AC7

86) chain G
residue 30
type
sequence L
description binding site for residue 967 G 401
source : AC7

87) chain G
residue 31
type
sequence T
description binding site for residue 967 G 401
source : AC7

88) chain F
residue 27
type
sequence T
description binding site for residue 967 H 401
source : AC8

89) chain F
residue 28
type
sequence G
description binding site for residue 967 H 401
source : AC8

90) chain H
residue 17
type
sequence V
description binding site for residue 967 H 401
source : AC8

91) chain H
residue 21
type
sequence G
description binding site for residue 967 H 401
source : AC8

92) chain H
residue 22
type
sequence R
description binding site for residue 967 H 401
source : AC8

93) chain H
residue 24
type
sequence A
description binding site for residue 967 H 401
source : AC8

94) chain H
residue 26
type
sequence G
description binding site for residue 967 H 401
source : AC8

95) chain H
residue 27
type
sequence T
description binding site for residue 967 H 401
source : AC8

96) chain H
residue 28
type
sequence G
description binding site for residue 967 H 401
source : AC8

97) chain H
residue 29
type
sequence E
description binding site for residue 967 H 401
source : AC8

98) chain H
residue 30
type
sequence L
description binding site for residue 967 H 401
source : AC8

99) chain H
residue 31
type
sequence T
description binding site for residue 967 H 401
source : AC8

100) chain A
residue 273-285
type prosite
sequence GKLRLLYECNPMA
description FBPASE Fructose-1-6-bisphosphatase active site. GKLrlLYEcnPMA
source prosite : PS00124

101) chain A
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

102) chain C
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

103) chain C
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

104) chain C
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

105) chain D
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

106) chain D
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

107) chain D
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

108) chain D
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

109) chain E
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

110) chain E
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

111) chain E
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

112) chain A
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

113) chain E
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

114) chain F
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

115) chain F
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

116) chain F
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

117) chain F
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

118) chain G
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

119) chain G
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

120) chain G
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

121) chain G
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

122) chain H
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

123) chain A
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

124) chain H
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

125) chain H
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

126) chain H
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

127) chain A
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

128) chain B
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

129) chain B
residue 27
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

130) chain B
residue 112
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

131) chain B
residue 140
type BINDING
sequence R
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

132) chain C
residue 17
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:7809062, ECO:0007744|PDB:1FTA
source Swiss-Prot : SWS_FT_FI1

133) chain B
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

134) chain B
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

135) chain B
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

136) chain B
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

137) chain B
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

138) chain C
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

139) chain C
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

140) chain C
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

141) chain C
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

142) chain A
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

143) chain C
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

144) chain C
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

145) chain D
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

146) chain D
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

147) chain D
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

148) chain D
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

149) chain D
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

150) chain D
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

151) chain A
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

152) chain E
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

153) chain E
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

154) chain E
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

155) chain E
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

156) chain E
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

157) chain E
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

158) chain F
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

159) chain F
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

160) chain F
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

161) chain A
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

162) chain F
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

163) chain F
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

164) chain F
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

165) chain G
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

166) chain G
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

167) chain G
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

168) chain G
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

169) chain G
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

170) chain G
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

171) chain A
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

172) chain H
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

173) chain H
residue 120
type BINDING
sequence L
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

174) chain H
residue 212
type BINDING
sequence N
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

175) chain H
residue 243
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

176) chain H
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

177) chain H
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

178) chain A
residue 264
type BINDING
sequence Y
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

179) chain A
residue 274
type BINDING
sequence K
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

180) chain B
residue 97
type BINDING
sequence E
description BINDING => ECO:0000250|UniProtKB:P00636
source Swiss-Prot : SWS_FT_FI2

181) chain A
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

182) chain D
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

183) chain D
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

184) chain D
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

185) chain E
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

186) chain E
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

187) chain E
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

188) chain F
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

189) chain F
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

190) chain F
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

191) chain G
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

192) chain A
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

193) chain G
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

194) chain G
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

195) chain H
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

196) chain H
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

197) chain H
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

198) chain A
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

199) chain B
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

200) chain B
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

201) chain B
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

202) chain C
residue 118
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

203) chain C
residue 121
type BINDING
sequence D
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

204) chain C
residue 280
type BINDING
sequence E
description BINDING => ECO:0007744|PDB:2FHY
source Swiss-Prot : SWS_FT_FI3

205) chain A
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

206) chain B
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

207) chain C
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

208) chain D
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

209) chain E
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

210) chain F
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

211) chain G
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

212) chain H
residue 150
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI5

213) chain A
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

214) chain E
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

215) chain F
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

216) chain F
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

217) chain G
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

218) chain G
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

219) chain H
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

220) chain H
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

221) chain A
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

222) chain B
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

223) chain B
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

224) chain C
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

225) chain C
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

226) chain D
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

227) chain D
residue 244
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

228) chain E
residue 215
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0000250|UniProtKB:Q9QXD6
source Swiss-Prot : SWS_FT_FI6

229) chain A
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

230) chain B
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

231) chain C
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

232) chain D
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

233) chain E
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

234) chain F
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

235) chain G
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7

236) chain H
residue 264
type MOD_RES
sequence Y
description Phosphotyrosine => ECO:0007744|PubMed:24275569
source Swiss-Prot : SWS_FT_FI7


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