eF-site ID 6d3m-ABFJ
PDB Code 6d3m
Chain A, B, F, J

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Title FT_T dioxygenase with bound quizalofop
Classification OXIDOREDUCTASE
Compound FT_T dioxygenase
Source (6D3M)
Sequence A:  NKYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAF
HTYQVIYFPGQAITNEQHIAFSRRFGPVDPVPILKSIEGY
PEVQMIRREANESSRFIGDDWHTDSTFLDAPPAAVVMRAI
EVPEYGGDTGFLSMYSAWETLSPTMQATIEGLNVVHSATK
VFGSLYQATNWRFSNTSVKVMDVDAGDRETVHPLVVTHPV
TGRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFDF
TCRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVA
GDKPSR
B:  KYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAFH
TYQVIYFPGQAITNEQHIAFSRRFGPVDPVPILKSIEGYP
EVQMIRREANESSRFIGDDWHTDSTFLDAPPAAVVMRAIE
VPEYGGDTGFLSMYSAWETLSPTMQATIEGLNVVHSATKV
FGSLYQATNWRFSNTSVKVMDVDAGDRETVHPLVVTHPVT
GRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFDFT
CRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVAG
DKPSR
F:  NKYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAF
HTYQVIYFPGQAITNEQHIAFSRRFGPVDPVPILKSIEGY
PEVQMIRREANESSRFIGDDWHTDSTFLDAPPAAVVMRAI
EVPEYGGDTGFLSMYSAWETLSPTMQATIEGLNVVHSATK
VFGSLYQATNWRFSNTSVKVMDVDAGDRETVHPLVVTHPV
TGRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFDF
TCRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVA
GDKPSR
J:  NKYRFIDVQPLTGVLGAEITGVDLREPLDDSTWNEILDAF
HTYQVIYFPGQAITNEQHIAFSRRFGPVDPVPILKSIEGY
PEVQMIRREANESSRFIGDDWHTDSTFLDAPPAAVVMRAI
EVPEYGGDTGFLSMYSAWETLSPTMQATIEGLNVVHSATK
VFGSLYQATNWRFSNTSVKVMDVDAGDRETVHPLVVTHPV
TGRRALYCNQVYCQKIQGMTDAESKSLLQFLYEHATKFDF
TCRVRWKKDQVLVWDNLCTMHRAVPDYAGKFRYLTRTTVA
GDKPSR
Description


Functional site

1) chain A
residue 111
type
sequence H
description binding site for residue CO A 301
source : AC1

2) chain A
residue 113
type
sequence D
description binding site for residue CO A 301
source : AC1

3) chain A
residue 270
type
sequence H
description binding site for residue CO A 301
source : AC1

4) chain A
residue 104
type
sequence R
description binding site for residue FTJ A 302
source : AC2

5) chain A
residue 107
type
sequence G
description binding site for residue FTJ A 302
source : AC2

6) chain A
residue 111
type
sequence H
description binding site for residue FTJ A 302
source : AC2

7) chain A
residue 113
type
sequence D
description binding site for residue FTJ A 302
source : AC2

8) chain A
residue 114
type
sequence S
description binding site for residue FTJ A 302
source : AC2

9) chain A
residue 169
type
sequence K
description binding site for residue FTJ A 302
source : AC2

10) chain A
residue 180
type
sequence W
description binding site for residue FTJ A 302
source : AC2

11) chain A
residue 182
type
sequence F
description binding site for residue FTJ A 302
source : AC2

12) chain A
residue 220
type
sequence V
description binding site for residue FTJ A 302
source : AC2

13) chain A
residue 221
type
sequence Y
description binding site for residue FTJ A 302
source : AC2

14) chain A
residue 95
type
sequence I
description binding site for residue AKG A 303
source : AC3

15) chain A
residue 107
type
sequence G
description binding site for residue AKG A 303
source : AC3

16) chain A
residue 111
type
sequence H
description binding site for residue AKG A 303
source : AC3

17) chain A
residue 113
type
sequence D
description binding site for residue AKG A 303
source : AC3

18) chain A
residue 126
type
sequence M
description binding site for residue AKG A 303
source : AC3

19) chain A
residue 138
type
sequence T
description binding site for residue AKG A 303
source : AC3

20) chain A
residue 270
type
sequence H
description binding site for residue AKG A 303
source : AC3

21) chain A
residue 272
type
sequence A
description binding site for residue AKG A 303
source : AC3

22) chain A
residue 281
type
sequence R
description binding site for residue AKG A 303
source : AC3

23) chain A
residue 285
type
sequence R
description binding site for residue AKG A 303
source : AC3

24) chain A
residue 72
type
sequence R
description binding site for residue CL A 304
source : AC4

25) chain A
residue 76
type
sequence P
description binding site for residue CL A 304
source : AC4

26) chain A
residue 77
type
sequence V
description binding site for residue CL A 304
source : AC4

27) chain B
residue 72
type
sequence R
description binding site for residue CL A 304
source : AC4

28) chain B
residue 76
type
sequence P
description binding site for residue CL A 304
source : AC4

29) chain B
residue 77
type
sequence V
description binding site for residue CL A 304
source : AC4

30) chain B
residue 111
type
sequence H
description binding site for residue CO B 301
source : AC5

31) chain B
residue 113
type
sequence D
description binding site for residue CO B 301
source : AC5

32) chain B
residue 270
type
sequence H
description binding site for residue CO B 301
source : AC5

33) chain B
residue 104
type
sequence R
description binding site for residue FTJ B 302
source : AC6

34) chain B
residue 107
type
sequence G
description binding site for residue FTJ B 302
source : AC6

35) chain B
residue 108
type
sequence D
description binding site for residue FTJ B 302
source : AC6

36) chain B
residue 109
type
sequence D
description binding site for residue FTJ B 302
source : AC6

37) chain B
residue 111
type
sequence H
description binding site for residue FTJ B 302
source : AC6

38) chain B
residue 113
type
sequence D
description binding site for residue FTJ B 302
source : AC6

39) chain B
residue 114
type
sequence S
description binding site for residue FTJ B 302
source : AC6

40) chain B
residue 169
type
sequence K
description binding site for residue FTJ B 302
source : AC6

41) chain B
residue 180
type
sequence W
description binding site for residue FTJ B 302
source : AC6

42) chain B
residue 182
type
sequence F
description binding site for residue FTJ B 302
source : AC6

43) chain B
residue 220
type
sequence V
description binding site for residue FTJ B 302
source : AC6

44) chain B
residue 221
type
sequence Y
description binding site for residue FTJ B 302
source : AC6

45) chain B
residue 95
type
sequence I
description binding site for residue AKG B 303
source : AC7

46) chain B
residue 111
type
sequence H
description binding site for residue AKG B 303
source : AC7

47) chain B
residue 113
type
sequence D
description binding site for residue AKG B 303
source : AC7

48) chain B
residue 126
type
sequence M
description binding site for residue AKG B 303
source : AC7

49) chain B
residue 138
type
sequence T
description binding site for residue AKG B 303
source : AC7

50) chain B
residue 270
type
sequence H
description binding site for residue AKG B 303
source : AC7

51) chain B
residue 272
type
sequence A
description binding site for residue AKG B 303
source : AC7

52) chain B
residue 281
type
sequence R
description binding site for residue AKG B 303
source : AC7

53) chain B
residue 285
type
sequence R
description binding site for residue AKG B 303
source : AC7

54) chain F
residue 111
type
sequence H
description binding site for residue CO F 301
source : AC8

55) chain F
residue 113
type
sequence D
description binding site for residue CO F 301
source : AC8

56) chain F
residue 270
type
sequence H
description binding site for residue CO F 301
source : AC8

57) chain F
residue 82
type
sequence I
description binding site for residue FTJ F 302
source : AC9

58) chain F
residue 104
type
sequence R
description binding site for residue FTJ F 302
source : AC9

59) chain F
residue 107
type
sequence G
description binding site for residue FTJ F 302
source : AC9

60) chain F
residue 111
type
sequence H
description binding site for residue FTJ F 302
source : AC9

61) chain F
residue 113
type
sequence D
description binding site for residue FTJ F 302
source : AC9

62) chain F
residue 114
type
sequence S
description binding site for residue FTJ F 302
source : AC9

63) chain F
residue 169
type
sequence K
description binding site for residue FTJ F 302
source : AC9

64) chain F
residue 180
type
sequence W
description binding site for residue FTJ F 302
source : AC9

65) chain F
residue 182
type
sequence F
description binding site for residue FTJ F 302
source : AC9

66) chain F
residue 220
type
sequence V
description binding site for residue FTJ F 302
source : AC9

67) chain F
residue 221
type
sequence Y
description binding site for residue FTJ F 302
source : AC9

68) chain F
residue 95
type
sequence I
description binding site for residue AKG F 303
source : AD1

69) chain F
residue 111
type
sequence H
description binding site for residue AKG F 303
source : AD1

70) chain F
residue 113
type
sequence D
description binding site for residue AKG F 303
source : AD1

71) chain F
residue 126
type
sequence M
description binding site for residue AKG F 303
source : AD1

72) chain F
residue 138
type
sequence T
description binding site for residue AKG F 303
source : AD1

73) chain F
residue 270
type
sequence H
description binding site for residue AKG F 303
source : AD1

74) chain F
residue 272
type
sequence A
description binding site for residue AKG F 303
source : AD1

75) chain F
residue 281
type
sequence R
description binding site for residue AKG F 303
source : AD1

76) chain F
residue 285
type
sequence R
description binding site for residue AKG F 303
source : AD1

77) chain F
residue 72
type
sequence R
description binding site for residue CL F 304
source : AD2

78) chain F
residue 76
type
sequence P
description binding site for residue CL F 304
source : AD2

79) chain F
residue 77
type
sequence V
description binding site for residue CL F 304
source : AD2

80) chain J
residue 72
type
sequence R
description binding site for residue CL F 304
source : AD2

81) chain J
residue 76
type
sequence P
description binding site for residue CL F 304
source : AD2

82) chain J
residue 77
type
sequence V
description binding site for residue CL F 304
source : AD2

83) chain J
residue 111
type
sequence H
description binding site for residue CO J 301
source : AD3

84) chain J
residue 113
type
sequence D
description binding site for residue CO J 301
source : AD3

85) chain J
residue 270
type
sequence H
description binding site for residue CO J 301
source : AD3

86) chain J
residue 104
type
sequence R
description binding site for residue FTJ J 302
source : AD4

87) chain J
residue 107
type
sequence G
description binding site for residue FTJ J 302
source : AD4

88) chain J
residue 108
type
sequence D
description binding site for residue FTJ J 302
source : AD4

89) chain J
residue 111
type
sequence H
description binding site for residue FTJ J 302
source : AD4

90) chain J
residue 113
type
sequence D
description binding site for residue FTJ J 302
source : AD4

91) chain J
residue 114
type
sequence S
description binding site for residue FTJ J 302
source : AD4

92) chain J
residue 169
type
sequence K
description binding site for residue FTJ J 302
source : AD4

93) chain J
residue 180
type
sequence W
description binding site for residue FTJ J 302
source : AD4

94) chain J
residue 182
type
sequence F
description binding site for residue FTJ J 302
source : AD4

95) chain J
residue 220
type
sequence V
description binding site for residue FTJ J 302
source : AD4

96) chain J
residue 221
type
sequence Y
description binding site for residue FTJ J 302
source : AD4

97) chain J
residue 95
type
sequence I
description binding site for residue AKG J 303
source : AD5

98) chain J
residue 107
type
sequence G
description binding site for residue AKG J 303
source : AD5

99) chain J
residue 111
type
sequence H
description binding site for residue AKG J 303
source : AD5

100) chain J
residue 113
type
sequence D
description binding site for residue AKG J 303
source : AD5

101) chain J
residue 126
type
sequence M
description binding site for residue AKG J 303
source : AD5

102) chain J
residue 138
type
sequence T
description binding site for residue AKG J 303
source : AD5

103) chain J
residue 270
type
sequence H
description binding site for residue AKG J 303
source : AD5

104) chain J
residue 272
type
sequence A
description binding site for residue AKG J 303
source : AD5

105) chain J
residue 281
type
sequence R
description binding site for residue AKG J 303
source : AD5

106) chain J
residue 285
type
sequence R
description binding site for residue AKG J 303
source : AD5

107) chain A
residue 111
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

108) chain B
residue 255
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

109) chain B
residue 270
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

110) chain B
residue 281
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

111) chain F
residue 111
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

112) chain F
residue 113
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

113) chain F
residue 138
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

114) chain F
residue 255
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

115) chain F
residue 270
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

116) chain F
residue 281
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

117) chain J
residue 111
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

118) chain A
residue 113
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

119) chain J
residue 113
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

120) chain J
residue 138
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

121) chain J
residue 255
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

122) chain J
residue 270
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

123) chain J
residue 281
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

124) chain A
residue 138
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

125) chain A
residue 255
type BINDING
sequence W
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

126) chain A
residue 270
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

127) chain A
residue 281
type BINDING
sequence R
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

128) chain B
residue 111
type BINDING
sequence H
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

129) chain B
residue 113
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

130) chain B
residue 138
type BINDING
sequence T
description BINDING => ECO:0000250|UniProtKB:P37610
source Swiss-Prot : SWS_FT_FI1

131) chain A
residue 221
type SITE
sequence Y
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

132) chain A
residue 285
type SITE
sequence R
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

133) chain B
residue 221
type SITE
sequence Y
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

134) chain B
residue 285
type SITE
sequence R
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

135) chain F
residue 221
type SITE
sequence Y
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

136) chain F
residue 285
type SITE
sequence R
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

137) chain J
residue 221
type SITE
sequence Y
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2

138) chain J
residue 285
type SITE
sequence R
description Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
source Swiss-Prot : SWS_FT_FI2


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