eF-site ID 6dyu-A
PDB Code 6dyu
Chain A

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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-((prop-2-yn-1-ylthio)methyl)pyrrolidin-3-ol
Classification HYDROLASE
Compound 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
Source (A0A1W0VQJ9_HELPX)
Sequence A:  QGVQKIGILGAMREEITPILELFGVDFEEIPLGGNVFHKG
VYHNKEIIVAYSKIGKVHSTLTTTSMILAFGVQKVLFSGV
AGSLVKDLKINDLLVATQLVQHDVDLSAFDHPLGFIPESA
IFIETSGSLNALAKKIANEQHIALKEGVIASGDQFVHSKE
RKEFLVSEFKASAVEMEGASVAFVCQKFGVPCCVLRSISD
NADEKAGMSFDEFLEKSAHTSAKFLKSMVDEL
Description


Functional site

1) chain A
residue 103
type
sequence D
description binding site for residue EDO A 301
source : AC1

2) chain A
residue 152
type
sequence Q
description binding site for residue EDO A 301
source : AC1

3) chain A
residue 153
type
sequence F
description binding site for residue EDO A 301
source : AC1

4) chain A
residue 9
type
sequence A
description binding site for residue OS2 A 302
source : AC2

5) chain A
residue 52
type
sequence I
description binding site for residue OS2 A 302
source : AC2

6) chain A
residue 78
type
sequence V
description binding site for residue OS2 A 302
source : AC2

7) chain A
residue 79
type
sequence A
description binding site for residue OS2 A 302
source : AC2

8) chain A
residue 80
type
sequence G
description binding site for residue OS2 A 302
source : AC2

9) chain A
residue 104
type
sequence L
description binding site for residue OS2 A 302
source : AC2

10) chain A
residue 109
type
sequence H
description binding site for residue OS2 A 302
source : AC2

11) chain A
residue 152
type
sequence Q
description binding site for residue OS2 A 302
source : AC2

12) chain A
residue 153
type
sequence F
description binding site for residue OS2 A 302
source : AC2

13) chain A
residue 154
type
sequence V
description binding site for residue OS2 A 302
source : AC2

14) chain A
residue 172
type
sequence V
description binding site for residue OS2 A 302
source : AC2

15) chain A
residue 173
type
sequence E
description binding site for residue OS2 A 302
source : AC2

16) chain A
residue 174
type
sequence M
description binding site for residue OS2 A 302
source : AC2

17) chain A
residue 175
type
sequence E
description binding site for residue OS2 A 302
source : AC2

18) chain A
residue 197
type
sequence S
description binding site for residue OS2 A 302
source : AC2

19) chain A
residue 198
type
sequence D
description binding site for residue OS2 A 302
source : AC2

20) chain A
residue 200
type
sequence A
description binding site for residue OS2 A 302
source : AC2

21) chain A
residue 208
type
sequence F
description binding site for residue OS2 A 302
source : AC2

22) chain A
residue 54
type
sequence K
description binding site for residue NH4 A 303
source : AC3

23) chain A
residue 54
type
sequence K
description binding site for residue NH4 A 303
source : AC3

24) chain A
residue 101
type
sequence D
description binding site for residue NH4 A 303
source : AC3

25) chain A
residue 101
type
sequence D
description binding site for residue NH4 A 303
source : AC3

26) chain A
residue 151
type
sequence D
description binding site for residue NH4 A 303
source : AC3

27) chain A
residue 151
type
sequence D
description binding site for residue NH4 A 303
source : AC3

28) chain A
residue 187
type
sequence G
description binding site for residue EDO B 302
source : AC5

29) chain A
residue 126
type
sequence S
description binding site for residue EDO B 303
source : AC6

30) chain A
residue 129
type
sequence A
description binding site for residue EDO B 303
source : AC6

31) chain A
residue 130
type
sequence L
description binding site for residue EDO B 303
source : AC6

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

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

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

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

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


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