eF-site ID 3mx5-ABC PDB Code 3mx5 Chain A, B, C click to enlarge Title Lassa fever virus nucleoprotein complexed with UTP 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 LEGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIA LYQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFAT QPGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKL IDIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKEEI TPHCALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFR B:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG NLSSQQLDQRRALLNMIGMSDGVVRVWDVKNAELLNNQFG TMPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTS DLDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGAC MLDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTP GERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVD LGLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIAL YQPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQ PGLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLI DIALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKEEIT PHCALMDCIMFDAAVSGGLNTSVLRAVLPRDMVFR C:  KSFLWTQSLRRELSGYCSNIKLQVVKDAQALLHGLDFSEV SNVQRLMRKERRDDNDLKRLRDLNQAVNNLVELKSTQQKS ILRVGTLTSDDLLILAADLEKLKSKVIRTERPLSAGVYMG NLSSQQLDQRRALLNMIGMDGVVRVWDVKNAELLNNQFGT MPSLTLACLTKQGQVDLNDAVQALTDLGLIYTAKYPNTSD LDRLTQSHPILNMIDTKKSSLNISGYNFSLGAAVKAGACM LDGGNMLETIKVSPQTMDGILKSILKVKKALGMFISDTPG ERNPYENILYKICLSGDGWPYIASRTSITGRAWENTVVDL GLTYSQLMTLKDAMLQLDPNAKTWMDIEGRPEDPVEIALY QPSSGCYIHFFREPTDLKQFKQDAKYSHGIDVTDLFATQP GLTSAVIDALPRNMVITCQGSDDIRKLLESQGRKDIKLID IALSKTDSRKYENAVWDQYKDLCHMHTGVVVEKKKEEITP HCALMDCIMFDAAVSGGLSVLRAVLPRDMVFR Description Functional site 1) chain A residue 117 type sequence E description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 2) chain A residue 120 type sequence L description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 3) chain A residue 172 type sequence L description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 4) chain A residue 176 type sequence F description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 5) chain A residue 177 type sequence G description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 6) chain A residue 178 type sequence T description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 7) chain A residue 238 type sequence S description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 8) chain A residue 239 type sequence L description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 9) chain A residue 240 type sequence N description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 10) chain A residue 241 type sequence I description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 11) chain A residue 253 type sequence K description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 12) chain A residue 300 type sequence R description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 13) chain A residue 309 type sequence K description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 14) chain A residue 323 type sequence R description BINDING SITE FOR RESIDUE UTP A 993 source : AC1 15) chain C residue 399 type sequence E description BINDING SITE FOR RESIDUE ZN C 570 source : AC2 16) chain C residue 506 type sequence C description BINDING SITE FOR RESIDUE ZN C 570 source : AC2 17) chain C residue 509 type sequence H description BINDING SITE FOR RESIDUE ZN C 570 source : AC2 18) chain C residue 529 type sequence C description BINDING SITE FOR RESIDUE ZN C 570 source : AC2 19) chain B residue 120 type sequence L description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 20) chain B residue 164 type sequence W description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 21) chain B residue 176 type sequence F description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 22) chain B residue 177 type sequence G description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 23) chain B residue 178 type sequence T description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 24) chain B residue 238 type sequence S description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 25) chain B residue 239 type sequence L description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 26) chain B residue 240 type sequence N description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 27) chain B residue 241 type sequence I description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 28) chain B residue 253 type sequence K description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 29) chain B residue 300 type sequence R description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 30) chain B residue 309 type sequence K description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 31) chain B residue 323 type sequence R description BINDING SITE FOR RESIDUE UTP B 993 source : AC3 32) chain B residue 399 type sequence E description BINDING SITE FOR RESIDUE ZN B 570 source : AC4 33) chain B residue 412 type sequence H description BINDING SITE FOR RESIDUE ZN B 570 source : AC4 34) chain B residue 506 type sequence C description BINDING SITE FOR RESIDUE ZN B 570 source : AC4 35) chain B residue 509 type sequence H description BINDING SITE FOR RESIDUE ZN B 570 source : AC4 36) chain B residue 529 type sequence C description BINDING SITE FOR RESIDUE ZN B 570 source : AC4 37) chain C residue 120 type sequence L description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 38) chain C residue 164 type sequence W description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 39) chain C residue 172 type sequence L description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 40) chain C residue 176 type sequence F description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 41) chain C residue 177 type sequence G description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 42) chain C residue 178 type sequence T description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 43) chain C residue 239 type sequence L description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 44) chain C residue 240 type sequence N description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 45) chain C residue 241 type sequence I description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 46) chain C residue 253 type sequence K description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 47) chain C residue 300 type sequence R description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 48) chain C residue 309 type sequence K description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 49) chain C residue 323 type sequence R description BINDING SITE FOR RESIDUE UTP C 993 source : AC5 50) chain A residue 399 type sequence E description BINDING SITE FOR RESIDUE ZN A 570 source : AC6 51) chain A residue 506 type sequence C description BINDING SITE FOR RESIDUE ZN A 570 source : AC6 52) chain A residue 509 type sequence H description BINDING SITE FOR RESIDUE ZN A 570 source : AC6 53) chain A residue 529 type sequence C description BINDING SITE FOR RESIDUE ZN A 570 source : AC6 54) 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 55) 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 56) 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 57) 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 58) 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 59) 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 60) 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 61) 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 62) 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 63) 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 64) 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 65) 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 66) 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 67) 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 68) 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 69) 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 70) 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 71) 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 72) 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 73) 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 74) 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 75) 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 76) 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 77) 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

Display surface Download Links