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8GTQ

cryo-EM structure of Omicron BA.5 S protein in complex with S2L20

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019064biological_processfusion of virus membrane with host plasma membrane
A0039654biological_processfusion of virus membrane with host endosome membrane
A0046813biological_processreceptor-mediated virion attachment to host cell
A0055036cellular_componentvirion membrane
A0075509biological_processendocytosis involved in viral entry into host cell
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019064biological_processfusion of virus membrane with host plasma membrane
B0039654biological_processfusion of virus membrane with host endosome membrane
B0046813biological_processreceptor-mediated virion attachment to host cell
B0055036cellular_componentvirion membrane
B0075509biological_processendocytosis involved in viral entry into host cell
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019064biological_processfusion of virus membrane with host plasma membrane
C0039654biological_processfusion of virus membrane with host endosome membrane
C0046813biological_processreceptor-mediated virion attachment to host cell
C0055036cellular_componentvirion membrane
C0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3597
DetailsTOPO_DOM: Extracellular => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
AGLN14-TYR1215
BGLN14-TYR1215
CGLN14-TYR1215

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
AILE1216-CYS1236
BILE1216-CYS1236
CILE1216-CYS1236

site_idSWS_FT_FI3
Number of Residues114
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsSITE: Cleavage; by host furin => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32142651, ECO:0000269|PubMed:32362314, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
AVAL687
BVAL687
CVAL687

site_idSWS_FT_FI5
Number of Residues3
DetailsSITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
APRO817
BPRO817
CPRO817

site_idSWS_FT_FI6
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20 => ECO:0000269|PubMed:34599882
ChainResidueDetails
AMET1237
ATHR1238
ASER1242
ACYS1243
ALYS1245
BMET1237
BTHR1238
BSER1242
BCYS1243
BLYS1245
CMET1237
CTHR1238
CSER1242
CCYS1243
CLYS1245

site_idSWS_FT_FI7
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20; partial => ECO:0000269|PubMed:34599882
ChainResidueDetails
ASER1249
ACYS1250
ASER1252
ALYS1255
APHE1256
BSER1249
BCYS1250
BSER1252
BLYS1255
BPHE1256
CSER1249
CCYS1250
CSER1252
CLYS1255
CPHE1256

site_idSWS_FT_FI8
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
AASN17
ATHR1160
ASER1175
BASN17
BTHR1160
BSER1175
CASN17
CTHR1160
CSER1175

site_idSWS_FT_FI9
Number of Residues15
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
AASN61
ATHR124
ATHR719
ASER803
ATHR1076
BASN61
BTHR124
BTHR719
BSER803
BTHR1076
CASN61
CTHR124
CTHR719
CSER803
CTHR1076

site_idSWS_FT_FI10
Number of Residues9
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
ATHR76
ASER151
ASER1196
BTHR76
BSER151
BSER1196
CTHR76
CSER151
CSER1196

site_idSWS_FT_FI11
Number of Residues21
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
ATHR167
ATHR284
ATHR333
ATHR345
ATHR618
ASER659
ATHR1100
BTHR167
BTHR284
BTHR333
BTHR345
BTHR618
BSER659
BTHR1100
CTHR167
CTHR284
CTHR333
CTHR345
CTHR618
CSER659
CTHR1100

site_idSWS_FT_FI12
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32363391, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
ATHR236
ASER711
BTHR236
BSER711
CTHR236
CSER711

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ASER325
BSER325
CSER325

site_idSWS_FT_FI14
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
AVAL327
BVAL327
CVAL327

site_idSWS_FT_FI15
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (hybrid) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
ASER605
BSER605
CSER605

site_idSWS_FT_FI16
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
ATHR678
ASER680
BTHR678
BSER680
CTHR678
CSER680

site_idSWS_FT_FI17
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32155444, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
ATHR1136
BTHR1136
CTHR1136

221051

PDB entries from 2024-06-12

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