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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

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
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
D0016020cellular_componentmembrane
D0019031cellular_componentviral envelope
D0019062biological_processvirion attachment to host cell
D0019064biological_processfusion of virus membrane with host plasma membrane
D0020002cellular_componenthost cell plasma 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
D0075509biological_processendocytosis involved in viral entry into host cell
G0016020cellular_componentmembrane
G0019031cellular_componentviral envelope
G0019062biological_processvirion attachment to host cell
G0019064biological_processfusion of virus membrane with host plasma membrane
G0020002cellular_componenthost cell plasma 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
G0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
ChainResidueDetails
ATYR204-HIS210
ETYR193-HIS199
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues193
DetailsDomain: {"description":"BetaCoV S1-CTD","evidences":[{"source":"PROSITE-ProRule","id":"PRU01269","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32132184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues21
DetailsRegion: {"description":"Putative superantigen; may bind T-cell receptor alpha/TRAC","evidences":[{"source":"PubMed","id":"32989130","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues222
DetailsRegion: {"description":"Receptor-binding domain (RBD)","evidences":[{"source":"PubMed","id":"32132184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues73
DetailsRegion: {"description":"Disordered","evidences":[{"source":"PubMed","id":"35108439","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsRegion: {"description":"Integrin-binding motif;","evidences":[{"source":"PubMed","id":"33102950","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues71
DetailsRegion: {"description":"Receptor-binding motif; binding to human ACE2","evidences":[{"source":"UniProtKB","id":"P59594","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsRegion: {"description":"Immunodominant HLA epitope recognized by the CD8+; called NF9 peptide","evidences":[{"source":"PubMed","id":"34171266","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues50
DetailsRegion: {"description":"Heptad repeat 1","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues44
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Cleavage; by host TMPRSS2 or CTSL","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32703818","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"34159616","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues5
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues7
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (HexNAc...) serine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (hybrid) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (GlcNAc...) threonine; by host GALNT1","evidences":[{"source":"PubMed","id":"34732583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"32155444","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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