eF-site ID 5ire-ABCDEF PDB Code 5ire Chain A, B, C, D, E, F Title The cryo-EM structure of Zika Virus Classification VIRUS Compound E protein Source ORGANISM_SCIENTIFIC: Zika virus; Sequence A:  IRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPT VDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEA YLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFA CSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHET DENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSD LYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKE ALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGA KGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAE TLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLIT ANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHW HRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNS LGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTK NGSISLMCLALGGVLIFLSTA B:  AVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNP GFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYS C:  IRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPT VDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEA YLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFA CSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHET DENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSD LYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKE ALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGA KGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAE TLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLIT ANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHW HRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNS LGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTK NGSISLMCLALGGVLIFLSTA D:  AVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNP GFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYS E:  IRCIGVSNRDFVEGMSGGTWVDVVLEHGGCVTVMAQDKPT VDIELVTTTVSNMAEVRSYCYEASISDMASDSRCPTQGEA YLDKQSDTQYVCKRTLVDRGWGNGCGLFGKGSLVTCAKFA CSKKMTGKSIQPENLEYRIMLSVHGSQHSGMIVNDTGHET DENRAKVEITPNSPRAEATLGGFGSLGLDCEPRTGLDFSD LYYLTMNNKHWLVHKEWFHDIPLPWHAGADTGTPHWNNKE ALVEFKDAHAKRQTVVVLGSQEGAVHTALAGALEAEMDGA KGRLSSGHLKCRLKMDKLRLKGVSYSLCTAAFTFTKIPAE TLHGTVTVEVQYAGTDGPCKVPAQMAVDMQTLTPVGRLIT ANPVITESTENSKMMLELDPPFGDSYIVIGVGEKKITHHW HRSGSTIGKAFEATVRGAKRMAVLGDTAWDFGSVGGALNS LGKGIHQIFGAAFKSLFGGMSWFSQILIGTLLMWLGLNTK NGSISLMCLALGGVLIFLSTA F:  AVTLPSHSTRKLQTRSQTWLESREYTKHLIRVENWIFRNP GFALAAAAIAWLLGSSTSQKVIYLVMILLIAPAYS Description (1)  E protein, M protein Functional site 1) chain B residue 75 type SITE sequence S description Cleavage; by host signal peptidase => ECO:0000250|UniProtKB:P06935 source Swiss-Prot : SWS_FT_FI4 2) chain D residue 75 type SITE sequence S description Cleavage; by host signal peptidase => ECO:0000250|UniProtKB:P06935 source Swiss-Prot : SWS_FT_FI4 3) chain F residue 75 type SITE sequence S description Cleavage; by host signal peptidase => ECO:0000250|UniProtKB:P06935 source Swiss-Prot : SWS_FT_FI4 4) chain B residue 35-54 type TRANSMEM sequence WIFRNPGFALAAAAIAWLLG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 5) chain D residue 35-54 type TRANSMEM sequence WIFRNPGFALAAAAIAWLLG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 35-54 type TRANSMEM sequence WIFRNPGFALAAAAIAWLLG description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 7) chain B residue 55-59 type TOPO_DOM sequence SSTSQ description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 8) chain D residue 55-59 type TOPO_DOM sequence SSTSQ description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 9) chain F residue 55-59 type TOPO_DOM sequence SSTSQ description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 10) chain E residue 456-477 type TOPO_DOM sequence LFGGMSWFSQILIGTLLMWLGL description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI2 11) chain B residue 60-75 type TRANSMEM sequence KVIYLVMILLIAPAYS description Helical => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 12) chain D residue 60-75 type TRANSMEM sequence KVIYLVMILLIAPAYS description Helical => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 13) chain F residue 60-75 type TRANSMEM sequence KVIYLVMILLIAPAYS description Helical => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 154 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:27093288, ECO:0000269|PubMed:27338953, ECO:0000269|PubMed:27882950, ECO:0000269|PubMed:29091758 source Swiss-Prot : SWS_FT_FI5 15) chain C residue 154 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:27093288, ECO:0000269|PubMed:27338953, ECO:0000269|PubMed:27882950, ECO:0000269|PubMed:29091758 source Swiss-Prot : SWS_FT_FI5 16) chain E residue 154 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:27093288, ECO:0000269|PubMed:27338953, ECO:0000269|PubMed:27882950, ECO:0000269|PubMed:29091758 source Swiss-Prot : SWS_FT_FI5 17) chain E residue 38 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6 18) chain E residue 281 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6 19) chain A residue 38 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6 20) chain A residue 281 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6 21) chain C residue 38 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6 22) chain C residue 281 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:A0A142I5B9 source Swiss-Prot : SWS_FT_FI6

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