eF-site ID 5q02-ABCD
PDB Code 5q02
Chain A, B, C, D

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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-(5-bromo-1,3-thiazol-2-yl)-3-[5-(1,2-oxazol-3-yl)thiophen-2-yl]sulfonylurea
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
RKAGIAHLYGIAGKKLDVLSNDLVMNMLKSSFATCVLVSE
EDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFG
IYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAM
DCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAK
DFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLV
YGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATT
GKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
D:  DVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAV
RKAGIAHLYGIAGKLDVLSNDLVMNMLKSSFATCVLVSEE
DKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGI
YRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMD
CGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYAKD
FDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVY
GGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTG
KEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHS
Description


Functional site

1) chain A
residue 17
type
sequence V
description binding site for residue 95J A 401
source : AC1

2) chain A
residue 18
type
sequence M
description binding site for residue 95J A 401
source : AC1

3) chain A
residue 20
type
sequence E
description binding site for residue 95J A 401
source : AC1

4) chain A
residue 21
type
sequence G
description binding site for residue 95J A 401
source : AC1

5) chain A
residue 22
type
sequence R
description binding site for residue 95J A 401
source : AC1

6) chain A
residue 26
type
sequence G
description binding site for residue 95J A 401
source : AC1

7) chain A
residue 27
type
sequence T
description binding site for residue 95J A 401
source : AC1

8) chain A
residue 28
type
sequence G
description binding site for residue 95J A 401
source : AC1

9) chain A
residue 29
type
sequence E
description binding site for residue 95J A 401
source : AC1

10) chain A
residue 30
type
sequence L
description binding site for residue 95J A 401
source : AC1

11) chain A
residue 31
type
sequence T
description binding site for residue 95J A 401
source : AC1

12) chain A
residue 177
type
sequence M
description binding site for residue 95J A 401
source : AC1

13) chain A
residue 179
type
sequence C
description binding site for residue 95J A 401
source : AC1

14) chain C
residue 27
type
sequence T
description binding site for residue 95J A 401
source : AC1

15) chain C
residue 28
type
sequence G
description binding site for residue 95J A 401
source : AC1

16) chain B
residue 17
type
sequence V
description binding site for residue 95J B 401
source : AC2

17) chain B
residue 18
type
sequence M
description binding site for residue 95J B 401
source : AC2

18) chain B
residue 20
type
sequence E
description binding site for residue 95J B 401
source : AC2

19) chain B
residue 21
type
sequence G
description binding site for residue 95J B 401
source : AC2

20) chain B
residue 22
type
sequence R
description binding site for residue 95J B 401
source : AC2

21) chain B
residue 26
type
sequence G
description binding site for residue 95J B 401
source : AC2

22) chain B
residue 27
type
sequence T
description binding site for residue 95J B 401
source : AC2

23) chain B
residue 28
type
sequence G
description binding site for residue 95J B 401
source : AC2

24) chain B
residue 29
type
sequence E
description binding site for residue 95J B 401
source : AC2

25) chain B
residue 30
type
sequence L
description binding site for residue 95J B 401
source : AC2

26) chain B
residue 31
type
sequence T
description binding site for residue 95J B 401
source : AC2

27) chain B
residue 177
type
sequence M
description binding site for residue 95J B 401
source : AC2

28) chain B
residue 179
type
sequence C
description binding site for residue 95J B 401
source : AC2

29) chain D
residue 27
type
sequence T
description binding site for residue 95J B 401
source : AC2

30) chain D
residue 28
type
sequence G
description binding site for residue 95J B 401
source : AC2

31) chain A
residue 27
type
sequence T
description binding site for residue 95J C 401
source : AC3

32) chain C
residue 18
type
sequence M
description binding site for residue 95J C 401
source : AC3

33) chain C
residue 20
type
sequence E
description binding site for residue 95J C 401
source : AC3

34) chain C
residue 21
type
sequence G
description binding site for residue 95J C 401
source : AC3

35) chain C
residue 22
type
sequence R
description binding site for residue 95J C 401
source : AC3

36) chain C
residue 26
type
sequence G
description binding site for residue 95J C 401
source : AC3

37) chain C
residue 27
type
sequence T
description binding site for residue 95J C 401
source : AC3

38) chain C
residue 28
type
sequence G
description binding site for residue 95J C 401
source : AC3

39) chain C
residue 29
type
sequence E
description binding site for residue 95J C 401
source : AC3

40) chain C
residue 30
type
sequence L
description binding site for residue 95J C 401
source : AC3

41) chain C
residue 31
type
sequence T
description binding site for residue 95J C 401
source : AC3

42) chain C
residue 177
type
sequence M
description binding site for residue 95J C 401
source : AC3

43) chain C
residue 179
type
sequence C
description binding site for residue 95J C 401
source : AC3

44) chain B
residue 27
type
sequence T
description binding site for residue 95J D 401
source : AC4

45) chain B
residue 28
type
sequence G
description binding site for residue 95J D 401
source : AC4

46) chain D
residue 17
type
sequence V
description binding site for residue 95J D 401
source : AC4

47) chain D
residue 18
type
sequence M
description binding site for residue 95J D 401
source : AC4

48) chain D
residue 20
type
sequence E
description binding site for residue 95J D 401
source : AC4

49) chain D
residue 21
type
sequence G
description binding site for residue 95J D 401
source : AC4

50) chain D
residue 22
type
sequence R
description binding site for residue 95J D 401
source : AC4

51) chain D
residue 26
type
sequence G
description binding site for residue 95J D 401
source : AC4

52) chain D
residue 27
type
sequence T
description binding site for residue 95J D 401
source : AC4

53) chain D
residue 28
type
sequence G
description binding site for residue 95J D 401
source : AC4

54) chain D
residue 29
type
sequence E
description binding site for residue 95J D 401
source : AC4

55) chain D
residue 30
type
sequence L
description binding site for residue 95J D 401
source : AC4

56) chain D
residue 31
type
sequence T
description binding site for residue 95J D 401
source : AC4

57) chain D
residue 177
type
sequence M
description binding site for residue 95J D 401
source : AC4

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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