eF-site ID 4tu0-ABCD
PDB Code 4tu0
Chain A, B, C, D

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Title CRYSTAL STRUCTURE OF CHIKUNGUNYA VIRUS NSP3 MACRO DOMAIN IN COMPLEX WITH A 2'-5' OLIGOADENYLATE TRIMER
Classification VIRAL PROTEIN
Compound Non-structural polyprotein 3
Source (4TU0)
Sequence A:  HHAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVY
KKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSE
SEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGK
DRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQM
RT
B:  HHAPSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVY
KKWPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSE
SEGDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGK
DRLTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQM
RT
C:  APSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKK
WPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESE
GDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDR
LTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMRT
D:  APSYRVKRMDIAKNDEECVVNAANPRGLPGDGVCKAVYKK
WPESFKNSATPVGTAKTVMCGTYPVIHAVGPNFSNYSESE
GDRELAAAYREVAKEVTRLGVNSVAIPLLSTGVYSGGKDR
LTQSLNHLFTAMDSTDADVVIYCRDKEWEKKISEAIQMR
Description


Functional site

1) chain B
residue 35
type
sequence V
description binding site for residue PEG B 201
source : AC1

2) chain B
residue 114
type
sequence G
description binding site for residue PEG B 201
source : AC1

3) chain C
residue 24
type
sequence A
description binding site for residue PEG C 201
source : AC2

4) chain C
residue 35
type
sequence V
description binding site for residue PEG C 201
source : AC2

5) chain C
residue 110
type
sequence L
description binding site for residue PEG C 201
source : AC2

6) chain C
residue 113
type
sequence T
description binding site for residue PEG C 201
source : AC2

7) chain C
residue 114
type
sequence G
description binding site for residue PEG C 201
source : AC2

8) chain C
residue 116
type
sequence Y
description binding site for residue PEG C 201
source : AC2

9) chain A
residue 12
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

10) chain B
residue 114
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

11) chain B
residue 115
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

12) chain B
residue 116
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

13) chain C
residue 12
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

14) chain C
residue 26
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

15) chain C
residue 34
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

16) chain C
residue 114
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

17) chain C
residue 115
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

18) chain C
residue 116
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

19) chain D
residue 12
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

20) chain A
residue 26
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

21) chain D
residue 26
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

22) chain D
residue 34
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

23) chain D
residue 114
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

24) chain D
residue 115
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

25) chain D
residue 116
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 34
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

27) chain A
residue 114
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

28) chain A
residue 115
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 116
type BINDING
sequence Y
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

30) chain B
residue 12
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

31) chain B
residue 26
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1

32) chain B
residue 34
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:19386706
source Swiss-Prot : SWS_FT_FI1


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