eF-site ID 3mwt-ABC
PDB Code 3mwt
Chain A, B, C

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Title Crystal structure of Lassa fever virus nucleoprotein in complex with Mn2+
Classification NUCLEAR PROTEIN
Compound Nucleoprotein
Source Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV) (NCAP_LASSJ)
Sequence A:  IKSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSE
VSNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQK
SILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYM
GNLSSQQLDQRRALLNMIGMDGVVRVWDVKNAELLNNQFG
TMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTS
DLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGAC
MLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTP
GERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVD
LGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIAL
YQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQ
PGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLI
DIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKEEITP
HCALMDCIMFDAAVSGGLTSVLRAVLPRDMVFR
B:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV
SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS
ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG
NLSSQQLDQRRALLNMIGMSDGVVRVWDVKNAELLNNQFG
TMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTS
DLDRLTQSHPILNMIDTKSSLNISGYNFSLGAAVKAGACM
LDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPG
ERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVDG
LTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIALYQ
PSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQPG
LTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLIDI
ALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKEEITPHC
ALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFR
C:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV
SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS
ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG
NLSSQQLDQRRALLNMIGMGVVRVWDVKNAELLNNQFGTM
PSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSDL
DRLTQSHPILNMIDSSLNISGYNFSLGAAVKAGACMLNML
ETIKVSPQTMDGILKSILKVKKALGMFISDTPGERNPYEN
ILYKICLSGDGWPYIASRTSITGRAWENTVVDGLTYSQLM
TLKDAMLQLDPNAKTWMDIEGRPEDPVEIALYQPSSGCYI
HFFREPTDLKQFKQDAKYSHGIDVTDLFATQPGLTSAVID
ALPRNMVITCQGSDDIRKLLESQGRKDIKLIDIALSKTDS
RKYENAVWDQYKDLCHMHTGVVVEKEEITPHCALMDCIMF
DAAVSGGLLRAVLPRDMVFR
Description


Functional site

1) chain A
residue 389
type
sequence D
description BINDING SITE FOR RESIDUE MN A 680
source : AC1

2) chain A
residue 391
type
sequence E
description BINDING SITE FOR RESIDUE MN A 680
source : AC1

3) chain A
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE MN A 680
source : AC1

4) chain A
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 690
source : AC2

5) chain A
residue 412
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 690
source : AC2

6) chain A
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 690
source : AC2

7) chain A
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 690
source : AC2

8) chain A
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 690
source : AC2

9) chain B
residue 389
type
sequence D
description BINDING SITE FOR RESIDUE MN B 680
source : AC3

10) chain B
residue 391
type
sequence E
description BINDING SITE FOR RESIDUE MN B 680
source : AC3

11) chain B
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE MN B 680
source : AC3

12) chain B
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 690
source : AC4

13) chain B
residue 412
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 690
source : AC4

14) chain B
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 690
source : AC4

15) chain B
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 690
source : AC4

16) chain B
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 690
source : AC4

17) chain C
residue 389
type
sequence D
description BINDING SITE FOR RESIDUE MN C 680
source : AC5

18) chain C
residue 391
type
sequence E
description BINDING SITE FOR RESIDUE MN C 680
source : AC5

19) chain C
residue 533
type
sequence D
description BINDING SITE FOR RESIDUE MN C 680
source : AC5

20) chain C
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 690
source : AC6

21) chain C
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 690
source : AC6

22) chain C
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 690
source : AC6

23) chain C
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 690
source : AC6

24) chain A
residue 389
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

25) chain A
residue 391
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

26) chain A
residue 533
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

27) chain B
residue 389
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

28) chain B
residue 391
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

29) chain B
residue 533
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

30) chain C
residue 389
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

31) chain C
residue 391
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

32) chain C
residue 533
type BINDING
sequence D
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835
source Swiss-Prot : SWS_FT_FI1

33) chain A
residue 399
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

34) chain C
residue 506
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

35) chain C
residue 509
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

36) chain C
residue 529
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

37) chain A
residue 506
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

38) chain A
residue 509
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

39) chain A
residue 529
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

40) chain B
residue 399
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

41) chain B
residue 506
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

42) chain B
residue 509
type BINDING
sequence H
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

43) chain B
residue 529
type BINDING
sequence C
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

44) chain C
residue 399
type BINDING
sequence E
description BINDING => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117, ECO:0000269|PubMed:21262835, ECO:0000269|PubMed:22937163, ECO:0000269|PubMed:23615902
source Swiss-Prot : SWS_FT_FI2

45) chain A
residue 466
type SITE
sequence D
description Important for exonuclease activity => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117
source Swiss-Prot : SWS_FT_FI3

46) chain B
residue 466
type SITE
sequence D
description Important for exonuclease activity => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117
source Swiss-Prot : SWS_FT_FI3

47) chain C
residue 466
type SITE
sequence D
description Important for exonuclease activity => ECO:0000255|HAMAP-Rule:MF_04085, ECO:0000269|PubMed:21085117
source Swiss-Prot : SWS_FT_FI3


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