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

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Title Nucleoprotein structure of lassa fever virus
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
HCALMDCIMFDAAVSGGLSVLRAVLPRDMVFR
B:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV
SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS
ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG
NLSSQQLDQRRALLNMIGMSDGVVRVWDVKNAELLNNQFG
TMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTS
DLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGAC
MLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTP
GERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVD
LGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIAL
YQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQ
PGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLI
DIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKEEIT
PHCALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFR
C:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV
SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS
ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG
NLSSQQLDQRRALLNMIGMDGVVRVWDVKNAELLNNQFGT
MPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSD
LDRLTQSHPILNMIDTSSLNISGYNFSLGAAVKAGACMLD
GNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPGERN
PYENILYKICLSGDGWPYIASRTSITGRAWENTVVDGLTY
SQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIALYQPSS
GCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQPGLTS
AVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLIDIALS
KTDSRKYENAVWDQYKDLCHMHTGVVVEKKEEITPHCALM
DCIMFDAAVSGGLVLRAVLPRDMVFR
Description


Functional site

1) chain A
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN A 570
source : AC1

2) chain A
residue 412
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 570
source : AC1

3) chain A
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 570
source : AC1

4) chain A
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 570
source : AC1

5) chain A
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 570
source : AC1

6) chain B
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN B 570
source : AC2

7) chain B
residue 412
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 570
source : AC2

8) chain B
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 570
source : AC2

9) chain B
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 570
source : AC2

10) chain B
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 570
source : AC2

11) chain C
residue 399
type
sequence E
description BINDING SITE FOR RESIDUE ZN C 570
source : AC3

12) chain C
residue 506
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 570
source : AC3

13) chain C
residue 509
type
sequence H
description BINDING SITE FOR RESIDUE ZN C 570
source : AC3

14) chain C
residue 529
type
sequence C
description BINDING SITE FOR RESIDUE ZN C 570
source : AC3

15) 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

16) 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

17) 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

18) 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

19) 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

20) 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

21) 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

22) 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

23) 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

24) 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

25) 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

26) 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

27) 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

28) 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

29) 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

30) 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

31) 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

32) 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

33) 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

34) 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

35) 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

36) 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

37) 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

38) 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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