eF-site ID 6dyy-ABCD
PDB Code 6dyy
Chain A, B, C, D

click to enlarge
Title Crystal structure of Helicobacter pylori 5'-methylthioadenosine/S-adenosyl homocysteine nucleosidase (MTAN) complexed with (3R,4S)-1-((4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl)-4-(((3-(1-butyl-1H-1,2,3-triazol-4-yl)propyl)thio)methyl)pyrrolidin-3-ol
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Source (A0A1W0VQJ9_HELPX)
Sequence A:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG
VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV
AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA
IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE
RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD
NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL
B:  VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVY
HNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAG
SLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESAIF
IETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKERK
EFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNA
DEKAGMSFDEFLEKSAHTSAKFLKSMVDEL
C:  VQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKGVY
HNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGVAG
SLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESAIF
IETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKERK
EFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISDNA
DEKAGMSFDEFLEKSAHTSAKFLKSMVDEL
D:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG
VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV
AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA
IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE
RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD
NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL
Description


Functional site

1) chain A
residue 123
type
sequence T
description binding site for residue EDO A 301
source : AC1

2) chain A
residue 125
type
sequence G
description binding site for residue EDO A 301
source : AC1

3) chain A
residue 126
type
sequence S
description binding site for residue EDO A 301
source : AC1

4) chain C
residue 209
type
sequence D
description binding site for residue EDO A 301
source : AC1

5) chain D
residue 107
type
sequence F
description binding site for residue EDO A 301
source : AC1

6) chain A
residue 229
type
sequence E
description binding site for residue MG A 302
source : AC2

7) chain A
residue 52
type
sequence I
description binding site for residue OS6 A 303
source : AC3

8) chain A
residue 78
type
sequence V
description binding site for residue OS6 A 303
source : AC3

9) chain A
residue 79
type
sequence A
description binding site for residue OS6 A 303
source : AC3

10) chain A
residue 80
type
sequence G
description binding site for residue OS6 A 303
source : AC3

11) chain A
residue 152
type
sequence Q
description binding site for residue OS6 A 303
source : AC3

12) chain A
residue 153
type
sequence F
description binding site for residue OS6 A 303
source : AC3

13) chain A
residue 154
type
sequence V
description binding site for residue OS6 A 303
source : AC3

14) chain A
residue 172
type
sequence V
description binding site for residue OS6 A 303
source : AC3

15) chain A
residue 173
type
sequence E
description binding site for residue OS6 A 303
source : AC3

16) chain A
residue 174
type
sequence M
description binding site for residue OS6 A 303
source : AC3

17) chain A
residue 175
type
sequence E
description binding site for residue OS6 A 303
source : AC3

18) chain A
residue 197
type
sequence S
description binding site for residue OS6 A 303
source : AC3

19) chain A
residue 198
type
sequence D
description binding site for residue OS6 A 303
source : AC3

20) chain A
residue 200
type
sequence A
description binding site for residue OS6 A 303
source : AC3

21) chain A
residue 208
type
sequence F
description binding site for residue OS6 A 303
source : AC3

22) chain B
residue 109
type
sequence H
description binding site for residue OS6 A 303
source : AC3

23) chain B
residue 115
type
sequence P
description binding site for residue OS6 A 303
source : AC3

24) chain B
residue 116
type
sequence E
description binding site for residue OS6 A 303
source : AC3

25) chain B
residue 123
type
sequence T
description binding site for residue EDO B 301
source : AC4

26) chain B
residue 125
type
sequence G
description binding site for residue EDO B 301
source : AC4

27) chain B
residue 126
type
sequence S
description binding site for residue EDO B 301
source : AC4

28) chain C
residue 107
type
sequence F
description binding site for residue EDO B 301
source : AC4

29) chain D
residue 209
type
sequence D
description binding site for residue EDO B 301
source : AC4

30) chain A
residue 106
type
sequence A
description binding site for residue EDO B 302
source : AC5

31) chain A
residue 107
type
sequence F
description binding site for residue EDO B 302
source : AC5

32) chain B
residue 205
type
sequence G
description binding site for residue EDO B 302
source : AC5

33) chain B
residue 206
type
sequence M
description binding site for residue EDO B 302
source : AC5

34) chain B
residue 209
type
sequence D
description binding site for residue EDO B 302
source : AC5

35) chain B
residue 138
type
sequence Q
description binding site for residue EDO B 303
source : AC6

36) chain B
residue 139
type
sequence H
description binding site for residue EDO B 303
source : AC6

37) chain B
residue 165
type
sequence S
description binding site for residue EDO B 303
source : AC6

38) chain B
residue 166
type
sequence E
description binding site for residue EDO B 303
source : AC6

39) chain B
residue 133
type
sequence K
description binding site for residue MG B 304
source : AC7

40) chain A
residue 104
type
sequence L
description binding site for residue OS6 B 305
source : AC8

41) chain A
residue 109
type
sequence H
description binding site for residue OS6 B 305
source : AC8

42) chain A
residue 115
type
sequence P
description binding site for residue OS6 B 305
source : AC8

43) chain B
residue 9
type
sequence A
description binding site for residue OS6 B 305
source : AC8

44) chain B
residue 52
type
sequence I
description binding site for residue OS6 B 305
source : AC8

45) chain B
residue 78
type
sequence V
description binding site for residue OS6 B 305
source : AC8

46) chain B
residue 79
type
sequence A
description binding site for residue OS6 B 305
source : AC8

47) chain B
residue 80
type
sequence G
description binding site for residue OS6 B 305
source : AC8

48) chain B
residue 152
type
sequence Q
description binding site for residue OS6 B 305
source : AC8

49) chain B
residue 153
type
sequence F
description binding site for residue OS6 B 305
source : AC8

50) chain B
residue 154
type
sequence V
description binding site for residue OS6 B 305
source : AC8

51) chain B
residue 172
type
sequence V
description binding site for residue OS6 B 305
source : AC8

52) chain B
residue 173
type
sequence E
description binding site for residue OS6 B 305
source : AC8

53) chain B
residue 174
type
sequence M
description binding site for residue OS6 B 305
source : AC8

54) chain B
residue 175
type
sequence E
description binding site for residue OS6 B 305
source : AC8

55) chain B
residue 197
type
sequence S
description binding site for residue OS6 B 305
source : AC8

56) chain B
residue 198
type
sequence D
description binding site for residue OS6 B 305
source : AC8

57) chain B
residue 208
type
sequence F
description binding site for residue OS6 B 305
source : AC8

58) chain C
residue 132
type
sequence K
description binding site for residue OS6 B 305
source : AC8

59) chain C
residue 32
type
sequence G
description binding site for residue EDO C 301
source : AC9

60) chain C
residue 33
type
sequence N
description binding site for residue EDO C 301
source : AC9

61) chain C
residue 34
type
sequence V
description binding site for residue EDO C 301
source : AC9

62) chain C
residue 49
type
sequence Y
description binding site for residue EDO C 301
source : AC9

63) chain A
residue 157
type
sequence K
description binding site for residue EDO C 302
source : AD1

64) chain C
residue 156
type
sequence S
description binding site for residue EDO C 302
source : AD1

65) chain C
residue 157
type
sequence K
description binding site for residue EDO C 302
source : AD1

66) chain C
residue 201
type
sequence D
description binding site for residue EDO C 302
source : AD1

67) chain C
residue 202
type
sequence E
description binding site for residue EDO C 302
source : AD1

68) chain A
residue 122
type
sequence E
description binding site for residue OS6 C 303
source : AD2

69) chain C
residue 9
type
sequence A
description binding site for residue OS6 C 303
source : AD2

70) chain C
residue 52
type
sequence I
description binding site for residue OS6 C 303
source : AD2

71) chain C
residue 78
type
sequence V
description binding site for residue OS6 C 303
source : AD2

72) chain C
residue 79
type
sequence A
description binding site for residue OS6 C 303
source : AD2

73) chain C
residue 80
type
sequence G
description binding site for residue OS6 C 303
source : AD2

74) chain C
residue 152
type
sequence Q
description binding site for residue OS6 C 303
source : AD2

75) chain C
residue 153
type
sequence F
description binding site for residue OS6 C 303
source : AD2

76) chain C
residue 154
type
sequence V
description binding site for residue OS6 C 303
source : AD2

77) chain C
residue 172
type
sequence V
description binding site for residue OS6 C 303
source : AD2

78) chain C
residue 173
type
sequence E
description binding site for residue OS6 C 303
source : AD2

79) chain C
residue 174
type
sequence M
description binding site for residue OS6 C 303
source : AD2

80) chain C
residue 175
type
sequence E
description binding site for residue OS6 C 303
source : AD2

81) chain C
residue 197
type
sequence S
description binding site for residue OS6 C 303
source : AD2

82) chain C
residue 198
type
sequence D
description binding site for residue OS6 C 303
source : AD2

83) chain C
residue 208
type
sequence F
description binding site for residue OS6 C 303
source : AD2

84) chain D
residue 107
type
sequence F
description binding site for residue OS6 C 303
source : AD2

85) chain D
residue 109
type
sequence H
description binding site for residue OS6 C 303
source : AD2

86) chain D
residue 32
type
sequence G
description binding site for residue EDO D 301
source : AD3

87) chain D
residue 33
type
sequence N
description binding site for residue EDO D 301
source : AD3

88) chain D
residue 34
type
sequence V
description binding site for residue EDO D 301
source : AD3

89) chain D
residue 49
type
sequence Y
description binding site for residue EDO D 301
source : AD3

90) chain C
residue 109
type
sequence H
description binding site for residue OS6 D 302
source : AD4

91) chain D
residue 9
type
sequence A
description binding site for residue OS6 D 302
source : AD4

92) chain D
residue 52
type
sequence I
description binding site for residue OS6 D 302
source : AD4

93) chain D
residue 78
type
sequence V
description binding site for residue OS6 D 302
source : AD4

94) chain D
residue 79
type
sequence A
description binding site for residue OS6 D 302
source : AD4

95) chain D
residue 80
type
sequence G
description binding site for residue OS6 D 302
source : AD4

96) chain D
residue 153
type
sequence F
description binding site for residue OS6 D 302
source : AD4

97) chain D
residue 154
type
sequence V
description binding site for residue OS6 D 302
source : AD4

98) chain D
residue 172
type
sequence V
description binding site for residue OS6 D 302
source : AD4

99) chain D
residue 173
type
sequence E
description binding site for residue OS6 D 302
source : AD4

100) chain D
residue 174
type
sequence M
description binding site for residue OS6 D 302
source : AD4

101) chain D
residue 175
type
sequence E
description binding site for residue OS6 D 302
source : AD4

102) chain D
residue 197
type
sequence S
description binding site for residue OS6 D 302
source : AD4

103) chain D
residue 198
type
sequence D
description binding site for residue OS6 D 302
source : AD4

104) chain D
residue 208
type
sequence F
description binding site for residue OS6 D 302
source : AD4

105) chain A
residue 13
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI1

106) chain B
residue 13
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI1

107) chain C
residue 13
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI1

108) chain D
residue 13
type ACT_SITE
sequence E
description Proton acceptor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI1

109) chain A
residue 198
type ACT_SITE
sequence D
description Proton donor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI2

110) chain B
residue 198
type ACT_SITE
sequence D
description Proton donor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI2

111) chain C
residue 198
type ACT_SITE
sequence D
description Proton donor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI2

112) chain D
residue 198
type ACT_SITE
sequence D
description Proton donor => ECO:0000305|PubMed:20954236
source Swiss-Prot : SWS_FT_FI2

113) chain A
residue 80
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

114) chain B
residue 80
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

115) chain C
residue 80
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

116) chain D
residue 80
type BINDING
sequence G
description BINDING => ECO:0000250
source Swiss-Prot : SWS_FT_FI3

117) chain A
residue 154
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI4

118) chain A
residue 174
type BINDING
sequence M
description
source Swiss-Prot : SWS_FT_FI4

119) chain B
residue 154
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI4

120) chain B
residue 174
type BINDING
sequence M
description
source Swiss-Prot : SWS_FT_FI4

121) chain C
residue 154
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI4

122) chain C
residue 174
type BINDING
sequence M
description
source Swiss-Prot : SWS_FT_FI4

123) chain D
residue 154
type BINDING
sequence V
description
source Swiss-Prot : SWS_FT_FI4

124) chain D
residue 174
type BINDING
sequence M
description
source Swiss-Prot : SWS_FT_FI4


Display surface

Download
Links