9DHY

Structure of SARS-CoV-2 spike in complex with antibody Fab COVIC-154

Functional Information from GO Data

Chain	GOid	namespace	contents
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
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
K	0005515	molecular_function	protein binding
K	0005886	cellular_component	plasma membrane
K	0007165	biological_process	signal transduction
K	0016020	cellular_component	membrane
K	0019031	cellular_component	viral envelope
K	0019062	biological_process	virion attachment to host cell
K	0019064	biological_process	fusion of virus membrane with host plasma membrane
K	0019081	biological_process	viral translation
K	0020002	cellular_component	host cell plasma membrane
K	0033644	cellular_component	host cell membrane
K	0039587	biological_process	symbiont-mediated-mediated suppression of host tetherin activity
K	0039654	biological_process	fusion of virus membrane with host endosome membrane
K	0039660	molecular_function	structural constituent of virion
K	0039663	biological_process	membrane fusion involved in viral entry into host cell
K	0042802	molecular_function	identical protein binding
K	0043655	cellular_component	host extracellular space
K	0044173	cellular_component	host cell endoplasmic reticulum-Golgi intermediate compartment membrane
K	0044228	cellular_component	host cell surface
K	0044423	cellular_component	virion component
K	0046598	biological_process	positive regulation of viral entry into host cell
K	0046718	biological_process	symbiont entry into host cell
K	0046789	molecular_function	host cell surface receptor binding
K	0046813	biological_process	receptor-mediated virion attachment to host cell
K	0048018	molecular_function	receptor ligand activity
K	0052170	biological_process	symbiont-mediated suppression of host innate immune response
K	0055036	cellular_component	virion membrane
K	0061025	biological_process	membrane fusion
K	0075509	biological_process	endocytosis involved in viral entry into host cell
K	0098670	biological_process	entry receptor-mediated virion attachment to host cell
K	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
C	SER685
F	SER685
K	SER685

---

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
C	ARG815
F	ARG815
K	ARG815

---

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
C	ASN17
C	ASN1158
C	ASN1173
F	ASN17
F	ASN1158
F	ASN1173
K	ASN17
K	ASN1158
K	ASN1173

---

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
C	ASN61
F	ASN1074
K	ASN61
K	ASN122
K	ASN717
K	ASN801
K	ASN1074
C	ASN122
C	ASN717
C	ASN801
C	ASN1074
F	ASN61
F	ASN122
F	ASN717
F	ASN801

---

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
C	ASN74
C	ASN149
C	ASN1194
F	ASN74
F	ASN149
F	ASN1194
K	ASN74
K	ASN149
K	ASN1194

---

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
C	ASN165
F	ASN331
F	ASN343
F	ASN616
F	ASN657
F	ASN1098
K	ASN165
K	ASN282
K	ASN331
K	ASN343
K	ASN616
C	ASN282
K	ASN657
K	ASN1098
C	ASN331
C	ASN343
C	ASN616
C	ASN657
C	ASN1098
F	ASN165
F	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
C	ASN234
C	ASN709
F	ASN234
F	ASN709
K	ASN234
K	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
C	THR323
F	THR323
K	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
C	SER325
F	SER325
K	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
C	ASN603
F	ASN603
K	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
C	THR676
C	THR678
F	THR676
F	THR678
K	THR676
K	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
C	ASN1134
F	ASN1134
K	ASN1134

---