eF-site ID 5pzr-ABCD
PDB Code 5pzr
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-(3-chlorophenyl)sulfonyl-3-[3-[3-[(3-chlorophenyl)sulfonylcarbamoylamino]propoxy]propyl]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
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 93S A 401
source : AC1

2) chain A
residue 18
type
sequence M
description binding site for residue 93S A 401
source : AC1

3) chain A
residue 21
type
sequence G
description binding site for residue 93S A 401
source : AC1

4) chain A
residue 22
type
sequence R
description binding site for residue 93S A 401
source : AC1

5) chain A
residue 26
type
sequence G
description binding site for residue 93S A 401
source : AC1

6) chain A
residue 27
type
sequence T
description binding site for residue 93S A 401
source : AC1

7) chain A
residue 28
type
sequence G
description binding site for residue 93S A 401
source : AC1

8) chain A
residue 29
type
sequence E
description binding site for residue 93S A 401
source : AC1

9) chain A
residue 30
type
sequence L
description binding site for residue 93S A 401
source : AC1

10) chain A
residue 31
type
sequence T
description binding site for residue 93S A 401
source : AC1

11) chain A
residue 177
type
sequence M
description binding site for residue 93S A 401
source : AC1

12) chain C
residue 17
type
sequence V
description binding site for residue 93S A 401
source : AC1

13) chain C
residue 18
type
sequence M
description binding site for residue 93S A 401
source : AC1

14) chain C
residue 21
type
sequence G
description binding site for residue 93S A 401
source : AC1

15) chain C
residue 22
type
sequence R
description binding site for residue 93S A 401
source : AC1

16) chain C
residue 26
type
sequence G
description binding site for residue 93S A 401
source : AC1

17) chain C
residue 27
type
sequence T
description binding site for residue 93S A 401
source : AC1

18) chain C
residue 28
type
sequence G
description binding site for residue 93S A 401
source : AC1

19) chain C
residue 29
type
sequence E
description binding site for residue 93S A 401
source : AC1

20) chain C
residue 30
type
sequence L
description binding site for residue 93S A 401
source : AC1

21) chain C
residue 31
type
sequence T
description binding site for residue 93S A 401
source : AC1

22) chain C
residue 177
type
sequence M
description binding site for residue 93S A 401
source : AC1

23) chain B
residue 17
type
sequence V
description binding site for residue 93S B 401
source : AC2

24) chain B
residue 21
type
sequence G
description binding site for residue 93S B 401
source : AC2

25) chain B
residue 22
type
sequence R
description binding site for residue 93S B 401
source : AC2

26) chain B
residue 26
type
sequence G
description binding site for residue 93S B 401
source : AC2

27) chain B
residue 27
type
sequence T
description binding site for residue 93S B 401
source : AC2

28) chain B
residue 28
type
sequence G
description binding site for residue 93S B 401
source : AC2

29) chain B
residue 29
type
sequence E
description binding site for residue 93S B 401
source : AC2

30) chain B
residue 30
type
sequence L
description binding site for residue 93S B 401
source : AC2

31) chain B
residue 31
type
sequence T
description binding site for residue 93S B 401
source : AC2

32) chain D
residue 17
type
sequence V
description binding site for residue 93S B 401
source : AC2

33) chain D
residue 18
type
sequence M
description binding site for residue 93S B 401
source : AC2

34) chain D
residue 21
type
sequence G
description binding site for residue 93S B 401
source : AC2

35) chain D
residue 22
type
sequence R
description binding site for residue 93S B 401
source : AC2

36) chain D
residue 26
type
sequence G
description binding site for residue 93S B 401
source : AC2

37) chain D
residue 27
type
sequence T
description binding site for residue 93S B 401
source : AC2

38) chain D
residue 28
type
sequence G
description binding site for residue 93S B 401
source : AC2

39) chain D
residue 29
type
sequence E
description binding site for residue 93S B 401
source : AC2

40) chain D
residue 30
type
sequence L
description binding site for residue 93S B 401
source : AC2

41) chain D
residue 31
type
sequence T
description binding site for residue 93S B 401
source : AC2

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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


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