Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6ZOY

Structure of Disulphide-stabilized SARS-CoV-2 Spike Protein Trimer (x1 disulphide-bond mutant, S383C, D985C, K986P, V987P, single Arg S1/S2 cleavage site) in Closed State

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0016020cellular_componentmembrane
A0019031cellular_componentviral envelope
A0019049biological_processvirus-mediated perturbation of host defense response
A0019062biological_processvirion attachment to host cell
A0019064biological_processfusion of virus membrane with host plasma membrane
A0019065biological_processreceptor-mediated endocytosis of virus by host cell
A0019081biological_processviral translation
A0020002cellular_componenthost cell plasma membrane
A0033644cellular_componenthost cell membrane
A0039503biological_processobsolete suppression by virus of host innate immune response
A0039587biological_processsuppression by virus 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
A0055036cellular_componentvirion membrane
A0061025biological_processmembrane fusion
A0075509biological_processendocytosis involved in viral entry into host cell
A0098670biological_processentry receptor-mediated virion attachment to host cell
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0016020cellular_componentmembrane
B0019031cellular_componentviral envelope
B0019049biological_processvirus-mediated perturbation of host defense response
B0019062biological_processvirion attachment to host cell
B0019064biological_processfusion of virus membrane with host plasma membrane
B0019065biological_processreceptor-mediated endocytosis of virus by host cell
B0019081biological_processviral translation
B0020002cellular_componenthost cell plasma membrane
B0033644cellular_componenthost cell membrane
B0039503biological_processobsolete suppression by virus of host innate immune response
B0039587biological_processsuppression by virus of host tetherin activity
B0039654biological_processfusion of virus membrane with host endosome membrane
B0039660molecular_functionstructural constituent of virion
B0039663biological_processmembrane fusion involved in viral entry into host cell
B0042802molecular_functionidentical protein binding
B0043655cellular_componenthost extracellular space
B0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
B0044228cellular_componenthost cell surface
B0044423cellular_componentvirion component
B0046598biological_processpositive regulation of viral entry into host cell
B0046718biological_processsymbiont entry into host cell
B0046789molecular_functionhost cell surface receptor binding
B0046813biological_processreceptor-mediated virion attachment to host cell
B0048018molecular_functionreceptor ligand activity
B0055036cellular_componentvirion membrane
B0061025biological_processmembrane fusion
B0075509biological_processendocytosis involved in viral entry into host cell
B0098670biological_processentry receptor-mediated virion attachment to host cell
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0007165biological_processsignal transduction
C0016020cellular_componentmembrane
C0019031cellular_componentviral envelope
C0019049biological_processvirus-mediated perturbation of host defense response
C0019062biological_processvirion attachment to host cell
C0019064biological_processfusion of virus membrane with host plasma membrane
C0019065biological_processreceptor-mediated endocytosis of virus by host cell
C0019081biological_processviral translation
C0020002cellular_componenthost cell plasma membrane
C0033644cellular_componenthost cell membrane
C0039503biological_processobsolete suppression by virus of host innate immune response
C0039587biological_processsuppression by virus of host tetherin activity
C0039654biological_processfusion of virus membrane with host endosome membrane
C0039660molecular_functionstructural constituent of virion
C0039663biological_processmembrane fusion involved in viral entry into host cell
C0042802molecular_functionidentical protein binding
C0043655cellular_componenthost extracellular space
C0044173cellular_componenthost cell endoplasmic reticulum-Golgi intermediate compartment membrane
C0044228cellular_componenthost cell surface
C0044423cellular_componentvirion component
C0046598biological_processpositive regulation of viral entry into host cell
C0046718biological_processsymbiont entry into host cell
C0046789molecular_functionhost cell surface receptor binding
C0046813biological_processreceptor-mediated virion attachment to host cell
C0048018molecular_functionreceptor ligand activity
C0055036cellular_componentvirion membrane
C0061025biological_processmembrane fusion
C0075509biological_processendocytosis involved in viral entry into host cell
C0098670biological_processentry receptor-mediated virion attachment to host cell
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
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
BSER689
CSER689
ASER689

site_idSWS_FT_FI2
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
BGLU819
CGLU819
AGLU819

site_idSWS_FT_FI3
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
APRO1162
AVAL1177
BASN17
BPRO1162
BVAL1177
CASN17
CPRO1162
CVAL1177
AASN17

site_idSWS_FT_FI4
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
ASER721
AILE805
AALA1078
BASN61
BASN122
BSER721
BILE805
BALA1078
CASN61
CASN122
CSER721
CILE805
CALA1078
AASN61
AASN122

site_idSWS_FT_FI5
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
CASN74
CASN149
CILE1198
AASN74
AASN149
AILE1198
BASN74
BASN149
BILE1198

site_idSWS_FT_FI6
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
AASN343
AASN616
AASN657
ATRP1102
BASN165
BASN282
BASN331
BASN343
BASN616
BASN657
BTRP1102
CASN165
CASN282
CASN331
CASN343
CASN616
CASN657
CTRP1102
AASN165
AASN282
AASN331

site_idSWS_FT_FI7
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
BALA713
CASN234
CALA713
AASN234
AALA713
BASN234

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ATHR323
BTHR323
CTHR323

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391
ChainResidueDetails
ASER325
BSER325
CSER325

site_idSWS_FT_FI10
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
AASN603
BASN603
CASN603

site_idSWS_FT_FI11
Number of Residues6
DetailsCARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269|PubMed:34732583
ChainResidueDetails
BTHR678
CTHR676
CTHR678
ATHR678
BTHR676
ATHR676

site_idSWS_FT_FI12
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
ATYR1138
BTYR1138
CTYR1138

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon