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7WG9

Delta Spike Trimer(1 RBD Up)

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-TYR1213
BGLN14-TYR1213
CGLN14-TYR1213

site_idSWS_FT_FI2
Number of Residues60
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
AILE1214-CYS1234
BILE1214-CYS1234
CILE1214-CYS1234

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
AVAL685
BVAL685
CVAL685

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
APHE815
BPHE815
CPHE815

site_idSWS_FT_FI6
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20 => ECO:0000269|PubMed:34599882
ChainResidueDetails
AMET1235
BLYS1243
CMET1235
CTHR1236
CSER1240
CCYS1241
CLYS1243
ATHR1236
ASER1240
ACYS1241
ALYS1243
BMET1235
BTHR1236
BSER1240
BCYS1241

site_idSWS_FT_FI7
Number of Residues15
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20; partial => ECO:0000269|PubMed:34599882
ChainResidueDetails
ASER1247
BPHE1254
CSER1247
CCYS1248
CSER1250
CLYS1253
CPHE1254
ACYS1248
ASER1250
ALYS1253
APHE1254
BSER1247
BCYS1248
BSER1250
BLYS1253

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
ATHR1158
ASER1173
BASN17
BTHR1158
BSER1173
CASN17
CTHR1158
CSER1173

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
BTHR1074
CASN61
CASN122
CTHR717
CSER801
CTHR1074
AASN122
ATHR717
ASER801
ATHR1074
BASN61
BASN122
BTHR717
BSER801

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
AASN74
AASN149
ASER1194
BASN74
BASN149
BSER1194
CASN74
CASN149
CSER1194

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
ATHR165
BTHR331
BTHR343
BTHR616
BSER657
BTHR1098
CTHR165
CTHR282
CTHR331
CTHR343
CTHR616
ATHR282
CSER657
CTHR1098
ATHR331
ATHR343
ATHR616
ASER657
ATHR1098
BTHR165
BTHR282

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
ATHR234
ASER709
BTHR234
BSER709
CTHR234
CSER709

site_idSWS_FT_FI13
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ASER323
BSER323
CSER323

site_idSWS_FT_FI14
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
AVAL325
BVAL325
CVAL325

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
ASER603
BSER603
CSER603

site_idSWS_FT_FI16
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
ATHR676
ASER678
BTHR676
BSER678
CTHR676
CSER678

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
ATHR1134
BTHR1134
CTHR1134

222415

PDB entries from 2024-07-10

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