8ZY3

Sarbecovirus BANAL-20-236 Spike Trimer in a Locked Conformation

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

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	ILE685
B	ILE685
C	ILE685

---

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	PHE815
B	PHE815
C	PHE815

---

site_id	SWS_FT_FI3
Number of Residues	9
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	ASN18
A	LEU1158
A	LYS1173
B	ASN18
B	LEU1158
B	LYS1173
C	ASN18
C	LEU1158
C	LYS1173

---

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	ASN62
B	CYS1074
C	ASN62
C	ASN122
C	GLU717
C	PRO801
C	CYS1074
A	ASN122
A	GLU717
A	PRO801
A	CYS1074
B	ASN62
B	ASN122
B	GLU717
B	PRO801

---

site_id	SWS_FT_FI5
Number of Residues	9
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	ALA75
A	LYS149
A	GLN1194
B	ALA75
B	LYS149
B	GLN1194
C	ALA75
C	LYS149
C	GLN1194

---

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	CYS165
B	LEU331
B	PHE343
B	VAL616
B	GLU657
B	GLN1098
C	CYS165
C	THR282
C	LEU331
C	PHE343
C	VAL616
A	THR282
C	GLU657
C	GLN1098
A	LEU331
A	PHE343
A	VAL616
A	GLU657
A	GLN1098
B	CYS165
B	THR282

---

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	ILE234
A	ASN709
B	ILE234
B	ASN709
C	ILE234
C	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	VAL323
B	VAL323
C	VAL323

---

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	PHE325
B	PHE325
C	PHE325

---

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	GLN603
B	GLN603
C	GLN603

---

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	SER676
A	SER678
B	SER676
B	SER678
C	SER676
C	SER678

---

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	GLN1134
B	GLN1134
C	GLN1134

---