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8YBS

State - I: Spike 2-up RBD with THSC20.HVTR04 (Fab4)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
D0016020cellular_componentmembrane
D0019031cellular_componentviral envelope
D0019062biological_processvirion attachment to host cell
D0020002cellular_componenthost cell plasma membrane
D0033644cellular_componenthost cell membrane
D0039654biological_processfusion of virus membrane with host endosome membrane
D0039663biological_processmembrane fusion involved in viral entry into host cell
D0042802molecular_functionidentical protein binding
D0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
D0044423cellular_componentvirion component
D0046598biological_processpositive regulation of viral entry into host cell
D0046718biological_processsymbiont entry into host cell
D0046789molecular_functionhost cell surface receptor binding
D0046813biological_processreceptor-mediated virion attachment to host cell
D0055036cellular_componentvirion membrane
G0016020cellular_componentmembrane
G0019031cellular_componentviral envelope
G0019062biological_processvirion attachment to host cell
G0020002cellular_componenthost cell plasma membrane
G0033644cellular_componenthost cell membrane
G0039654biological_processfusion of virus membrane with host endosome membrane
G0039663biological_processmembrane fusion involved in viral entry into host cell
G0042802molecular_functionidentical protein binding
G0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
G0044423cellular_componentvirion component
G0046598biological_processpositive regulation of viral entry into host cell
G0046718biological_processsymbiont entry into host cell
G0046789molecular_functionhost cell surface receptor binding
G0046813biological_processreceptor-mediated virion attachment to host cell
G0055036cellular_componentvirion membrane
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH
ChainResidueDetails
ETYR193-HIS199
ATYR204-HIS210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1199
DetailsTOPO_DOM: Extracellular => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
BGLN14-PRO1213

site_idSWS_FT_FI2
Number of Residues20
DetailsTRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
BTRP1214-LEU1234

site_idSWS_FT_FI3
Number of Residues38
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255|HAMAP-Rule:MF_04099
ChainResidueDetails
BCYS1235-THR1273

site_idSWS_FT_FI4
Number of Residues1
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
BARG685

site_idSWS_FT_FI5
Number of Residues1
DetailsSITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32703818, ECO:0000269|PubMed:34159616
ChainResidueDetails
BARG815

site_idSWS_FT_FI6
Number of Residues5
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20 => ECO:0000269|PubMed:34599882
ChainResidueDetails
BCYS1235
BCYS1236
BCYS1240
BCYS1241
BCYS1243

site_idSWS_FT_FI7
Number of Residues5
DetailsLIPID: S-palmitoyl cysteine; by host ZDHHC20; partial => ECO:0000269|PubMed:34599882
ChainResidueDetails
BCYS1247
BCYS1248
BCYS1250
BCYS1253
BCYS1254

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04099, ECO:0000269|PubMed:32366695, ECO:0000269|PubMed:32979942
ChainResidueDetails
BASN17
BASN1158
BASN1173

site_idSWS_FT_FI9
Number of Residues5
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
BASN61
BASN122
BASN717
BASN801
BASN1074

site_idSWS_FT_FI10
Number of Residues3
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
BASN74
BASN149
BASN1194

site_idSWS_FT_FI11
Number of Residues7
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
BASN165
BASN282
BASN331
BASN343
BASN616
BASN657
BASN1098

site_idSWS_FT_FI12
Number of Residues2
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
BASN234
BASN709

site_idSWS_FT_FI13
Number of Residues1
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BTHR323

site_idSWS_FT_FI14
Number of Residues1
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
BSER325

site_idSWS_FT_FI15
Number of Residues1
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
BASN603

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
BTHR676
BTHR678

site_idSWS_FT_FI17
Number of Residues1
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
BASN1134

236620

PDB entries from 2025-05-28

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