eF-site ID 3lkz-AB
PDB Code 3lkz
Chain A, B

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Title Structural and functional analyses of a conserved hydrophobic pocket of flavivirus methyltransferase
Classification VIRAL PROTEIN
Compound Non-structural protein 5
Source West Nile virus (WNV) (Q9Q6P4_WNV)
Sequence A:  GRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHAR
KEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGR
GGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIV
TMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRV
LEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGG
GLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRM
EKRTWKGPQYEEDVNLGSGTRA
B:  GRTLGEVWKERLNQMTKEEFTRYRKEAIIEVDRSAAKHAR
KEGNVTGGHPVSRGTAKLRWLVERRFLEPVGKVIDLGCGR
GGWCYYMATQKRVQEVRGYTKGGPGHEEPQLVQSYGWNIV
TMKSGVDVFYRPSECCDTLLCDIGESSSSAEVEEHRTIRV
LEMVEDWLHRGPREFCVKVLCPYMPKVIEKMELLQRRYGG
GLVRNPLSRNSTHEMYWVSRASGNVVHSVNMTSQVLLGRM
EKRTWKGPQYEEDVNLGSGTRA
Description


Functional site

1) chain A
residue 56
type
sequence S
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

2) chain A
residue 58
type
sequence G
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

3) chain A
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

4) chain A
residue 82
type
sequence C
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

5) chain A
residue 83
type
sequence G
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

6) chain A
residue 86
type
sequence G
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

7) chain A
residue 87
type
sequence W
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

8) chain A
residue 105
type
sequence K
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

9) chain A
residue 110
type
sequence H
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

10) chain A
residue 111
type
sequence E
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

11) chain A
residue 130
type
sequence V
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

12) chain A
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

13) chain A
residue 132
type
sequence V
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

14) chain A
residue 133
type
sequence F
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

15) chain A
residue 146
type
sequence D
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

16) chain A
residue 147
type
sequence I
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

17) chain A
residue 149
type
sequence E
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

18) chain B
residue 200
type
sequence R
description BINDING SITE FOR RESIDUE SFG A 301
source : AC1

19) chain A
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 302
source : AC2

20) chain A
residue 246
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 302
source : AC2

21) chain A
residue 247
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 302
source : AC2

22) chain A
residue 248
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 302
source : AC2

23) chain B
residue 177
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 302
source : AC2

24) chain A
residue 200
type
sequence R
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

25) chain B
residue 56
type
sequence S
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

26) chain B
residue 58
type
sequence G
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

27) chain B
residue 81
type
sequence G
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

28) chain B
residue 82
type
sequence C
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

29) chain B
residue 83
type
sequence G
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

30) chain B
residue 86
type
sequence G
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

31) chain B
residue 87
type
sequence W
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

32) chain B
residue 104
type
sequence T
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

33) chain B
residue 105
type
sequence K
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

34) chain B
residue 110
type
sequence H
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

35) chain B
residue 111
type
sequence E
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

36) chain B
residue 130
type
sequence V
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

37) chain B
residue 131
type
sequence D
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

38) chain B
residue 132
type
sequence V
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

39) chain B
residue 133
type
sequence F
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

40) chain B
residue 146
type
sequence D
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

41) chain B
residue 149
type
sequence E
description BINDING SITE FOR RESIDUE SFG B 301
source : AC3

42) chain A
residue 177
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 302
source : AC4

43) chain B
residue 159
type
sequence H
description BINDING SITE FOR RESIDUE GOL B 302
source : AC4

44) chain B
residue 246
type
sequence K
description BINDING SITE FOR RESIDUE GOL B 302
source : AC4

45) chain B
residue 247
type
sequence R
description BINDING SITE FOR RESIDUE GOL B 302
source : AC4

46) chain B
residue 248
type
sequence T
description BINDING SITE FOR RESIDUE GOL B 302
source : AC4

47) chain A
residue 56
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P03314
source Swiss-Prot : SWS_FT_FI11

48) chain B
residue 56
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P03314
source Swiss-Prot : SWS_FT_FI11

49) chain A
residue 61
type ACT_SITE
sequence K
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

50) chain A
residue 146
type ACT_SITE
sequence D
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

51) chain A
residue 182
type ACT_SITE
sequence K
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

52) chain A
residue 218
type ACT_SITE
sequence E
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

53) chain B
residue 61
type ACT_SITE
sequence K
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

54) chain B
residue 146
type ACT_SITE
sequence D
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

55) chain B
residue 182
type ACT_SITE
sequence K
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

56) chain B
residue 218
type ACT_SITE
sequence E
description For 2'-O-MTase activity => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI1

57) chain A
residue 16
type SITE
sequence L
description mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI7

58) chain A
residue 19
type SITE
sequence M
description mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI7

59) chain B
residue 16
type SITE
sequence L
description mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI7

60) chain B
residue 19
type SITE
sequence M
description mRNA cap binding; via carbonyl oxygen => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI7

61) chain A
residue 24
type SITE
sequence F
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI8

62) chain B
residue 24
type SITE
sequence F
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI8

63) chain A
residue 61
type SITE
sequence K
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

64) chain A
residue 182
type SITE
sequence K
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

65) chain A
residue 218
type SITE
sequence E
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

66) chain B
residue 61
type SITE
sequence K
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

67) chain B
residue 182
type SITE
sequence K
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

68) chain B
residue 218
type SITE
sequence E
description Essential for 2'-O-methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI9

69) chain A
residue 86
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

70) chain A
residue 87
type BINDING
sequence W
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

71) chain A
residue 131
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

72) chain A
residue 132
type BINDING
sequence V
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

73) chain B
residue 86
type BINDING
sequence G
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

74) chain B
residue 87
type BINDING
sequence W
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

75) chain B
residue 131
type BINDING
sequence D
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

76) chain B
residue 132
type BINDING
sequence V
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0007744|PDB:2OY0
source Swiss-Prot : SWS_FT_FI3

77) chain A
residue 104
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

78) chain A
residue 105
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

79) chain A
residue 147
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

80) chain A
residue 220
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

81) chain B
residue 104
type BINDING
sequence T
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

82) chain B
residue 105
type BINDING
sequence K
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

83) chain B
residue 147
type BINDING
sequence I
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

84) chain B
residue 220
type BINDING
sequence Y
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI4

85) chain A
residue 111
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI5

86) chain A
residue 146
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI5

87) chain B
residue 111
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI5

88) chain B
residue 146
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI5

89) chain A
residue 13
type SITE
sequence K
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

90) chain B
residue 150
type SITE
sequence S
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

91) chain B
residue 213
type SITE
sequence R
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

92) chain B
residue 215
type SITE
sequence S
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

93) chain A
residue 17
type SITE
sequence N
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

94) chain A
residue 28
type SITE
sequence R
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

95) chain A
residue 150
type SITE
sequence S
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

96) chain A
residue 213
type SITE
sequence R
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

97) chain A
residue 215
type SITE
sequence S
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

98) chain B
residue 13
type SITE
sequence K
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

99) chain B
residue 17
type SITE
sequence N
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

100) chain B
residue 28
type SITE
sequence R
description mRNA cap binding => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI6

101) chain A
residue 146
type SITE
sequence D
description Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI10

102) chain B
residue 146
type SITE
sequence D
description Essential for 2'-O-methyltransferase and N-7 methyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU00924
source Swiss-Prot : SWS_FT_FI10

103) chain A
residue 56
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI2

104) chain B
residue 56
type BINDING
sequence S
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00924, ECO:0000269|PubMed:17267492
source Swiss-Prot : SWS_FT_FI2


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