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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7CWS

SARS-CoV-2 Spike Proteins Trimer in Complex with FC05 and H014 Fabs Cocktail

Functional Information from GO Data
ChainGOidnamespacecontents
O0005515molecular_functionprotein binding
O0005886cellular_componentplasma membrane
O0007165biological_processsignal transduction
O0016020cellular_componentmembrane
O0019031cellular_componentviral envelope
O0019062biological_processvirion attachment to host cell
O0019064biological_processfusion of virus membrane with host plasma membrane
O0020002cellular_componenthost cell plasma membrane
O0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
O0039654biological_processfusion of virus membrane with host endosome membrane
O0039660molecular_functionstructural constituent of virion
O0039663biological_processmembrane fusion involved in viral entry into host cell
O0042802molecular_functionidentical protein binding
O0043655cellular_componenthost extracellular space
O0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
O0044228cellular_componenthost cell surface
O0044423cellular_componentvirion component
O0046598biological_processpositive regulation of viral entry into host cell
O0046718biological_processsymbiont entry into host cell
O0046789molecular_functionhost cell surface receptor binding
O0046813biological_processreceptor-mediated virion attachment to host cell
O0048018molecular_functionreceptor ligand activity
O0052031biological_processsymbiont-mediated perturbation of host defense response
O0052170biological_processsymbiont-mediated suppression of host innate immune response
O0055036cellular_componentvirion membrane
O0061025biological_processmembrane fusion
O0075509biological_processendocytosis involved in viral entry into host cell
O0098670biological_processentry receptor-mediated virion attachment to host cell
O0141146biological_processsymbiont-mediated disruption of host tissue
Q0005515molecular_functionprotein binding
Q0005886cellular_componentplasma membrane
Q0007165biological_processsignal transduction
Q0016020cellular_componentmembrane
Q0019031cellular_componentviral envelope
Q0019062biological_processvirion attachment to host cell
Q0019064biological_processfusion of virus membrane with host plasma membrane
Q0020002cellular_componenthost cell plasma membrane
Q0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
Q0039654biological_processfusion of virus membrane with host endosome membrane
Q0039660molecular_functionstructural constituent of virion
Q0039663biological_processmembrane fusion involved in viral entry into host cell
Q0042802molecular_functionidentical protein binding
Q0043655cellular_componenthost extracellular space
Q0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
Q0044228cellular_componenthost cell surface
Q0044423cellular_componentvirion component
Q0046598biological_processpositive regulation of viral entry into host cell
Q0046718biological_processsymbiont entry into host cell
Q0046789molecular_functionhost cell surface receptor binding
Q0046813biological_processreceptor-mediated virion attachment to host cell
Q0048018molecular_functionreceptor ligand activity
Q0052031biological_processsymbiont-mediated perturbation of host defense response
Q0052170biological_processsymbiont-mediated suppression of host innate immune response
Q0055036cellular_componentvirion membrane
Q0061025biological_processmembrane fusion
Q0075509biological_processendocytosis involved in viral entry into host cell
Q0098670biological_processentry receptor-mediated virion attachment to host cell
Q0141146biological_processsymbiont-mediated disruption of host tissue
R0005515molecular_functionprotein binding
R0005886cellular_componentplasma membrane
R0007165biological_processsignal transduction
R0016020cellular_componentmembrane
R0019031cellular_componentviral envelope
R0019062biological_processvirion attachment to host cell
R0019064biological_processfusion of virus membrane with host plasma membrane
R0020002cellular_componenthost cell plasma membrane
R0039587biological_processsymbiont-mediated-mediated suppression of host tetherin activity
R0039654biological_processfusion of virus membrane with host endosome membrane
R0039660molecular_functionstructural constituent of virion
R0039663biological_processmembrane fusion involved in viral entry into host cell
R0042802molecular_functionidentical protein binding
R0043655cellular_componenthost extracellular space
R0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
R0044228cellular_componenthost cell surface
R0044423cellular_componentvirion component
R0046598biological_processpositive regulation of viral entry into host cell
R0046718biological_processsymbiont entry into host cell
R0046789molecular_functionhost cell surface receptor binding
R0046813biological_processreceptor-mediated virion attachment to host cell
R0048018molecular_functionreceptor ligand activity
R0052031biological_processsymbiont-mediated perturbation of host defense response
R0052170biological_processsymbiont-mediated suppression of host innate immune response
R0055036cellular_componentvirion membrane
R0061025biological_processmembrane fusion
R0075509biological_processendocytosis involved in viral entry into host cell
R0098670biological_processentry receptor-mediated virion attachment to host cell
R0141146biological_processsymbiont-mediated disruption of host tissue
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues360
DetailsRegion: {"description":"Disordered","evidences":[{"source":"PubMed","id":"35108439","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
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_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 Residues150
DetailsRegion: {"description":"Heptad repeat 1","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues132
DetailsCoiled coil: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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":"32366695","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32979942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
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_FI10
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"},{"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_FI11
Number of Residues21
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_FI12
Number of Residues6
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_FI13
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GalNAc) threonine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (HexNAc...) serine; by host","evidences":[{"source":"PubMed","id":"32363391","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
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_FI16
Number of Residues3
DetailsGlycosylation: {"description":"O-linked (GlcNAc...) threonine; by host GALNT1","evidences":[{"source":"PubMed","id":"34732583","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
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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