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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8YRO

SARS-CoV-2 Delta Spike in complex with JL-8C

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019062biological_processvirion attachment to host cell
A0019064biological_processfusion of virus membrane with host plasma membrane
A0020002cellular_componenthost cell plasma membrane
A0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
A0039654biological_processfusion of virus membrane with host endosome membrane
A0039660molecular_functionstructural constituent of virion
A0039663biological_processmembrane fusion involved in viral entry into host cell
A0042802molecular_functionidentical protein binding
A0043655cellular_componenthost extracellular space
A0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
A0044228cellular_componenthost cell surface
A0044423cellular_componentvirion component
A0046598biological_processpositive regulation of viral entry into host cell
A0046718biological_processsymbiont entry into host cell
A0046789molecular_functionhost cell surface receptor binding
A0046813biological_processreceptor-mediated virion attachment to host cell
A0048018molecular_functionreceptor ligand activity
A0052031biological_processsymbiont-mediated perturbation of host defense response
A0052170biological_processsymbiont-mediated suppression of host innate immune response
A0055036cellular_componentvirion membrane
A0061025biological_processmembrane fusion
A0075509biological_processendocytosis involved in viral entry into host cell
A0098670biological_processentry receptor-mediated virion attachment to host cell
A0141146biological_processsymbiont-mediated disruption of host tissue
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0007165biological_processsignal transduction
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
D0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
D0039654biological_processfusion of virus membrane with host endosome membrane
D0039660molecular_functionstructural constituent of virion
D0039663biological_processmembrane fusion involved in viral entry into host cell
D0042802molecular_functionidentical protein binding
D0043655cellular_componenthost extracellular space
D0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
D0044228cellular_componenthost cell surface
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
D0048018molecular_functionreceptor ligand activity
D0052031biological_processsymbiont-mediated perturbation of host defense response
D0052170biological_processsymbiont-mediated suppression of host innate immune response
D0055036cellular_componentvirion membrane
D0061025biological_processmembrane fusion
D0075509biological_processendocytosis involved in viral entry into host cell
D0098670biological_processentry receptor-mediated virion attachment to host cell
D0141146biological_processsymbiont-mediated disruption of host tissue
P0005515molecular_functionprotein binding
P0005886cellular_componentplasma membrane
P0007165biological_processsignal transduction
P0016020cellular_componentmembrane
P0019031cellular_componentviral envelope
P0019062biological_processvirion attachment to host cell
P0019064biological_processfusion of virus membrane with host plasma membrane
P0020002cellular_componenthost cell plasma membrane
P0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
P0039654biological_processfusion of virus membrane with host endosome membrane
P0039660molecular_functionstructural constituent of virion
P0039663biological_processmembrane fusion involved in viral entry into host cell
P0042802molecular_functionidentical protein binding
P0043655cellular_componenthost extracellular space
P0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
P0044228cellular_componenthost cell surface
P0044423cellular_componentvirion component
P0046598biological_processpositive regulation of viral entry into host cell
P0046718biological_processsymbiont entry into host cell
P0046789molecular_functionhost cell surface receptor binding
P0046813biological_processreceptor-mediated virion attachment to host cell
P0048018molecular_functionreceptor ligand activity
P0052031biological_processsymbiont-mediated perturbation of host defense response
P0052170biological_processsymbiont-mediated suppression of host innate immune response
P0055036cellular_componentvirion membrane
P0061025biological_processmembrane fusion
P0075509biological_processendocytosis involved in viral entry into host cell
P0098670biological_processentry receptor-mediated virion attachment to host cell
P0141146biological_processsymbiont-mediated disruption of host tissue
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsRegion: {"description":"Putative superantigen; may bind T-cell receptor alpha/TRAC","evidences":[{"source":"PubMed","id":"32989130","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues92
DetailsRegion: {"description":"Disordered","evidences":[{"source":"PubMed","id":"35108439","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"Integrin-binding motif;","evidences":[{"source":"PubMed","id":"33102950","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues24
DetailsRegion: {"description":"Immunodominant HLA epitope recognized by the CD8+; called NF9 peptide","evidences":[{"source":"PubMed","id":"34171266","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues132
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues3
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_FI7
Number of Residues15
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_FI8
Number of Residues20
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_FI9
Number of Residues5
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_FI10
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (HexNAc...) serine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues3
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_FI13
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GlcNAc...) threonine; by host GALNT1","evidences":[{"source":"PubMed","id":"34732583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
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

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PDB entries from 2025-12-24

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