Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7CWS

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

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0005515	molecular_function	protein binding
O	0005886	cellular_component	plasma membrane
O	0007165	biological_process	signal transduction
O	0016020	cellular_component	membrane
O	0019031	cellular_component	viral envelope
O	0019062	biological_process	virion attachment to host cell
O	0019064	biological_process	fusion of virus membrane with host plasma membrane
O	0019065	biological_process	receptor-mediated endocytosis of virus by host cell
O	0019081	biological_process	viral translation
O	0020002	cellular_component	host cell plasma membrane
O	0039587	biological_process	suppression by virus of host tetherin activity
O	0039654	biological_process	fusion of virus membrane with host endosome membrane
O	0039660	molecular_function	structural constituent of virion
O	0042802	molecular_function	identical protein binding
O	0043655	cellular_component	host extracellular space
O	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
O	0044228	cellular_component	host cell surface
O	0046598	biological_process	positive regulation of viral entry into host cell
O	0046718	biological_process	symbiont entry into host cell
O	0046789	molecular_function	host cell surface receptor binding
O	0046813	biological_process	receptor-mediated virion attachment to host cell
O	0048018	molecular_function	receptor ligand activity
O	0052170	biological_process	symbiont-mediated suppression of host innate immune response
O	0055036	cellular_component	virion membrane
O	0061025	biological_process	membrane fusion
O	0075509	biological_process	endocytosis involved in viral entry into host cell
O	0098670	biological_process	entry receptor-mediated virion attachment to host cell
Q	0005515	molecular_function	protein binding
Q	0005886	cellular_component	plasma membrane
Q	0007165	biological_process	signal transduction
Q	0016020	cellular_component	membrane
Q	0019031	cellular_component	viral envelope
Q	0019062	biological_process	virion attachment to host cell
Q	0019064	biological_process	fusion of virus membrane with host plasma membrane
Q	0019065	biological_process	receptor-mediated endocytosis of virus by host cell
Q	0019081	biological_process	viral translation
Q	0020002	cellular_component	host cell plasma membrane
Q	0039587	biological_process	suppression by virus of host tetherin activity
Q	0039654	biological_process	fusion of virus membrane with host endosome membrane
Q	0039660	molecular_function	structural constituent of virion
Q	0042802	molecular_function	identical protein binding
Q	0043655	cellular_component	host extracellular space
Q	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
Q	0044228	cellular_component	host cell surface
Q	0046598	biological_process	positive regulation of viral entry into host cell
Q	0046718	biological_process	symbiont entry into host cell
Q	0046789	molecular_function	host cell surface receptor binding
Q	0046813	biological_process	receptor-mediated virion attachment to host cell
Q	0048018	molecular_function	receptor ligand activity
Q	0052170	biological_process	symbiont-mediated suppression of host innate immune response
Q	0055036	cellular_component	virion membrane
Q	0061025	biological_process	membrane fusion
Q	0075509	biological_process	endocytosis involved in viral entry into host cell
Q	0098670	biological_process	entry receptor-mediated virion attachment to host cell
R	0005515	molecular_function	protein binding
R	0005886	cellular_component	plasma membrane
R	0007165	biological_process	signal transduction
R	0016020	cellular_component	membrane
R	0019031	cellular_component	viral envelope
R	0019062	biological_process	virion attachment to host cell
R	0019064	biological_process	fusion of virus membrane with host plasma membrane
R	0019065	biological_process	receptor-mediated endocytosis of virus by host cell
R	0019081	biological_process	viral translation
R	0020002	cellular_component	host cell plasma membrane
R	0039587	biological_process	suppression by virus of host tetherin activity
R	0039654	biological_process	fusion of virus membrane with host endosome membrane
R	0039660	molecular_function	structural constituent of virion
R	0042802	molecular_function	identical protein binding
R	0043655	cellular_component	host extracellular space
R	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
R	0044228	cellular_component	host cell surface
R	0046598	biological_process	positive regulation of viral entry into host cell
R	0046718	biological_process	symbiont entry into host cell
R	0046789	molecular_function	host cell surface receptor binding
R	0046813	biological_process	receptor-mediated virion attachment to host cell
R	0048018	molecular_function	receptor ligand activity
R	0052170	biological_process	symbiont-mediated suppression of host innate immune response
R	0055036	cellular_component	virion membrane
R	0061025	biological_process	membrane fusion
R	0075509	biological_process	endocytosis involved in viral entry into host cell
R	0098670	biological_process	entry receptor-mediated virion attachment to host cell

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: 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

Chain	Residue	Details
O	ARG685
Q	ARG685
R	ARG685

site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Cleavage; by host TMPRSS2 or CTSL => ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32703818, ECO:0000269\|PubMed:34159616

Chain	Residue	Details
O	ARG815
Q	ARG815
R	ARG815

site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) (complex) asparagine; by host => ECO:0000255\|HAMAP-Rule:MF_04099, ECO:0000269\|PubMed:32366695, ECO:0000269\|PubMed:32979942

Chain	Residue	Details
O	ASN17
Q	ASN17
R	ASN17

site_id	SWS_FT_FI4
Number of Residues	15
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN61
Q	ASN1074
R	ASN61
R	ASN122
R	ASN717
R	ASN801
R	ASN1074
O	ASN122
O	ASN717
O	ASN801
O	ASN1074
Q	ASN61
Q	ASN122
Q	ASN717
Q	ASN801

site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN74
O	ASN149
Q	ASN74
Q	ASN149
R	ASN74
R	ASN149

site_id	SWS_FT_FI6
Number of Residues	21
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN165
Q	ASN331
Q	ASN343
Q	ASN616
Q	ASN657
Q	ASN1098
R	ASN165
R	ASN282
R	ASN331
R	ASN343
R	ASN616
O	ASN282
R	ASN657
R	ASN1098
O	ASN331
O	ASN343
O	ASN616
O	ASN657
O	ASN1098
Q	ASN165
Q	ASN282

site_id	SWS_FT_FI7
Number of Residues	6
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN234
O	ASN709
Q	ASN234
Q	ASN709
R	ASN234
R	ASN709

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
O	THR323
Q	THR323
R	THR323

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
O	SER325
Q	SER325
R	SER325

site_id	SWS_FT_FI10
Number of Residues	3
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN603
Q	ASN603
R	ASN603

site_id	SWS_FT_FI11
Number of Residues	6
Details	CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269\|PubMed:34732583

Chain	Residue	Details
O	THR676
O	THR678
Q	THR676
Q	THR678
R	THR676
R	THR678

site_id	SWS_FT_FI12
Number of Residues	3
Details	CARBOHYD: 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

Chain	Residue	Details
O	ASN1134
Q	ASN1134
R	ASN1134

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)