8GDR

SARS-Cov2 S protein structure in complex with neutralizing monoclonal antibody 002-S21B10

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0007165	biological_process	signal transduction
A	0016020	cellular_component	membrane
A	0019031	cellular_component	viral envelope
A	0019062	biological_process	virion attachment to host cell
A	0019064	biological_process	fusion of virus membrane with host plasma membrane
A	0019081	biological_process	viral translation
A	0020002	cellular_component	host cell plasma membrane
A	0033644	cellular_component	host cell membrane
A	0039587	biological_process	symbiont-mediated-mediated suppression of host tetherin activity
A	0039654	biological_process	fusion of virus membrane with host endosome membrane
A	0039660	molecular_function	structural constituent of virion
A	0039663	biological_process	membrane fusion involved in viral entry into host cell
A	0042802	molecular_function	identical protein binding
A	0043655	cellular_component	host extracellular space
A	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
A	0044228	cellular_component	host cell surface
A	0044423	cellular_component	virion component
A	0046598	biological_process	positive regulation of viral entry into host cell
A	0046718	biological_process	symbiont entry into host cell
A	0046789	molecular_function	host cell surface receptor binding
A	0046813	biological_process	receptor-mediated virion attachment to host cell
A	0048018	molecular_function	receptor ligand activity
A	0052170	biological_process	symbiont-mediated suppression of host innate immune response
A	0055036	cellular_component	virion membrane
A	0061025	biological_process	membrane fusion
A	0075509	biological_process	endocytosis involved in viral entry into host cell
A	0098670	biological_process	entry receptor-mediated virion attachment to host cell
A	0141146	biological_process	symbiont-mediated disruption of host tissue
E	0005515	molecular_function	protein binding
E	0005886	cellular_component	plasma membrane
E	0007165	biological_process	signal transduction
E	0016020	cellular_component	membrane
E	0019031	cellular_component	viral envelope
E	0019062	biological_process	virion attachment to host cell
E	0019064	biological_process	fusion of virus membrane with host plasma membrane
E	0019081	biological_process	viral translation
E	0020002	cellular_component	host cell plasma membrane
E	0033644	cellular_component	host cell membrane
E	0039587	biological_process	symbiont-mediated-mediated suppression of host tetherin activity
E	0039654	biological_process	fusion of virus membrane with host endosome membrane
E	0039660	molecular_function	structural constituent of virion
E	0039663	biological_process	membrane fusion involved in viral entry into host cell
E	0042802	molecular_function	identical protein binding
E	0043655	cellular_component	host extracellular space
E	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
E	0044228	cellular_component	host cell surface
E	0044423	cellular_component	virion component
E	0046598	biological_process	positive regulation of viral entry into host cell
E	0046718	biological_process	symbiont entry into host cell
E	0046789	molecular_function	host cell surface receptor binding
E	0046813	biological_process	receptor-mediated virion attachment to host cell
E	0048018	molecular_function	receptor ligand activity
E	0052170	biological_process	symbiont-mediated suppression of host innate immune response
E	0055036	cellular_component	virion membrane
E	0061025	biological_process	membrane fusion
E	0075509	biological_process	endocytosis involved in viral entry into host cell
E	0098670	biological_process	entry receptor-mediated virion attachment to host cell
E	0141146	biological_process	symbiont-mediated disruption of host tissue
F	0005515	molecular_function	protein binding
F	0005886	cellular_component	plasma membrane
F	0007165	biological_process	signal transduction
F	0016020	cellular_component	membrane
F	0019031	cellular_component	viral envelope
F	0019062	biological_process	virion attachment to host cell
F	0019064	biological_process	fusion of virus membrane with host plasma membrane
F	0019081	biological_process	viral translation
F	0020002	cellular_component	host cell plasma membrane
F	0033644	cellular_component	host cell membrane
F	0039587	biological_process	symbiont-mediated-mediated suppression of host tetherin activity
F	0039654	biological_process	fusion of virus membrane with host endosome membrane
F	0039660	molecular_function	structural constituent of virion
F	0039663	biological_process	membrane fusion involved in viral entry into host cell
F	0042802	molecular_function	identical protein binding
F	0043655	cellular_component	host extracellular space
F	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
F	0044228	cellular_component	host cell surface
F	0044423	cellular_component	virion component
F	0046598	biological_process	positive regulation of viral entry into host cell
F	0046718	biological_process	symbiont entry into host cell
F	0046789	molecular_function	host cell surface receptor binding
F	0046813	biological_process	receptor-mediated virion attachment to host cell
F	0048018	molecular_function	receptor ligand activity
F	0052170	biological_process	symbiont-mediated suppression of host innate immune response
F	0055036	cellular_component	virion membrane
F	0061025	biological_process	membrane fusion
F	0075509	biological_process	endocytosis involved in viral entry into host cell
F	0098670	biological_process	entry receptor-mediated virion attachment to host cell
F	0141146	biological_process	symbiont-mediated disruption of host tissue

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCQVTH

Chain	Residue	Details
D	TYR195-HIS201
C	TYR200-HIS206

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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
A	GLY685
E	GLY685
F	GLY685

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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
A	ARG815
E	ARG815
F	ARG815

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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
A	ASN17
E	ASN17
F	ASN17

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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
A	ASN61
E	ASN1074
F	ASN61
F	ASN122
F	ASN717
F	ASN801
F	ASN1074
A	ASN122
A	ASN717
A	ASN801
A	ASN1074
E	ASN61
E	ASN122
E	ASN717
E	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
A	ASN74
A	ASN149
E	ASN74
E	ASN149
F	ASN74
F	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
A	ASN165
E	ASN331
E	ASN343
E	ASN616
E	ASN657
E	ASN1098
F	ASN165
F	ASN282
F	ASN331
F	ASN343
F	ASN616
A	ASN282
F	ASN657
F	ASN1098
A	ASN331
A	ASN343
A	ASN616
A	ASN657
A	ASN1098
E	ASN165
E	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
A	ASN234
A	ASN709
E	ASN234
E	ASN709
F	ASN234
F	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
A	THR323
E	THR323
F	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
A	SER325
E	SER325
F	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
A	ASN603
E	ASN603
F	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
A	THR676
A	THR678
E	THR676
E	THR678
F	THR676
F	THR678

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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
A	ASN1134
E	ASN1134
F	ASN1134

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