Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7V7H

Cryo-EM structure of SARS-CoV-2 S-Kappa variant (B.1.617.1), dimer of S trimer conformation 1

This is a non-PDB format compatible entry.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016020	cellular_component	membrane
A	0019031	cellular_component	viral envelope
A	0019064	biological_process	fusion of virus membrane with host plasma membrane
A	0039654	biological_process	fusion of virus membrane with host endosome membrane
A	0046813	biological_process	receptor-mediated virion attachment to host cell
A	0055036	cellular_component	virion membrane
A	0075509	biological_process	endocytosis involved in viral entry into host cell
B	0016020	cellular_component	membrane
B	0019031	cellular_component	viral envelope
B	0019064	biological_process	fusion of virus membrane with host plasma membrane
B	0039654	biological_process	fusion of virus membrane with host endosome membrane
B	0046813	biological_process	receptor-mediated virion attachment to host cell
B	0055036	cellular_component	virion membrane
B	0075509	biological_process	endocytosis involved in viral entry into host cell
C	0016020	cellular_component	membrane
C	0019031	cellular_component	viral envelope
C	0019064	biological_process	fusion of virus membrane with host plasma membrane
C	0039654	biological_process	fusion of virus membrane with host endosome membrane
C	0046813	biological_process	receptor-mediated virion attachment to host cell
C	0055036	cellular_component	virion membrane
C	0075509	biological_process	endocytosis involved in viral entry into host cell
D	0016020	cellular_component	membrane
D	0019031	cellular_component	viral envelope
D	0019064	biological_process	fusion of virus membrane with host plasma membrane
D	0039654	biological_process	fusion of virus membrane with host endosome membrane
D	0046813	biological_process	receptor-mediated virion attachment to host cell
D	0055036	cellular_component	virion membrane
D	0075509	biological_process	endocytosis involved in viral entry into host cell
E	0016020	cellular_component	membrane
E	0019031	cellular_component	viral envelope
E	0019064	biological_process	fusion of virus membrane with host plasma membrane
E	0039654	biological_process	fusion of virus membrane with host endosome membrane
E	0046813	biological_process	receptor-mediated virion attachment to host cell
E	0055036	cellular_component	virion membrane
E	0075509	biological_process	endocytosis involved in viral entry into host cell
F	0016020	cellular_component	membrane
F	0019031	cellular_component	viral envelope
F	0019064	biological_process	fusion of virus membrane with host plasma membrane
F	0039654	biological_process	fusion of virus membrane with host endosome membrane
F	0046813	biological_process	receptor-mediated virion attachment to host cell
F	0055036	cellular_component	virion membrane
F	0075509	biological_process	endocytosis involved in viral entry into host cell

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
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	SER685
B	SER685
C	SER685
D	SER685
E	SER685
F	SER685

site_id	SWS_FT_FI2
Number of Residues	6
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
B	ARG815
C	ARG815
D	ARG815
E	ARG815
F	ARG815

site_id	SWS_FT_FI3
Number of Residues	18
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
D	ASN17
D	ASN1158
D	ASN1173
E	ASN17
E	ASN1158
E	ASN1173
F	ASN17
F	ASN1158
F	ASN1173
A	ASN1158
A	ASN1173
B	ASN17
B	ASN1158
B	ASN1173
C	ASN17
C	ASN1158
C	ASN1173

site_id	SWS_FT_FI4
Number of Residues	30
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
B	ASN1074
C	ASN61
C	ASN122
C	ASN717
C	ASN801
C	ASN1074
D	ASN61
D	ASN122
D	ASN717
D	ASN801
A	ASN122
D	ASN1074
E	ASN61
E	ASN122
E	ASN717
E	ASN801
E	ASN1074
F	ASN61
F	ASN122
F	ASN717
F	ASN801
A	ASN717
F	ASN1074
A	ASN801
A	ASN1074
B	ASN61
B	ASN122
B	ASN717
B	ASN801

site_id	SWS_FT_FI5
Number of Residues	18
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
D	ASN74
D	ASN149
D	ASN1194
E	ASN74
E	ASN149
E	ASN1194
F	ASN74
F	ASN149
F	ASN1194
A	ASN149
A	ASN1194
B	ASN74
B	ASN149
B	ASN1194
C	ASN74
C	ASN149
C	ASN1194

site_id	SWS_FT_FI6
Number of Residues	42
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
B	ASN331
B	ASN343
B	ASN616
B	ASN657
B	ASN1098
C	ASN165
C	ASN282
C	ASN331
C	ASN343
C	ASN616
A	ASN282
C	ASN657
C	ASN1098
D	ASN165
D	ASN282
D	ASN331
D	ASN343
D	ASN616
D	ASN657
D	ASN1098
E	ASN165
A	ASN331
E	ASN282
E	ASN331
E	ASN343
E	ASN616
E	ASN657
E	ASN1098
F	ASN165
F	ASN282
F	ASN331
F	ASN343
A	ASN343
F	ASN616
F	ASN657
F	ASN1098
A	ASN616
A	ASN657
A	ASN1098
B	ASN165
B	ASN282

site_id	SWS_FT_FI7
Number of Residues	12
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
E	ASN709
F	ASN234
F	ASN709
A	ASN709
B	ASN234
B	ASN709
C	ASN234
C	ASN709
D	ASN234
D	ASN709
E	ASN234

site_id	SWS_FT_FI8
Number of Residues	6
Details	CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
A	THR323
B	THR323
C	THR323
D	THR323
E	THR323
F	THR323

site_id	SWS_FT_FI9
Number of Residues	6
Details	CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
A	SER325
B	SER325
C	SER325
D	SER325
E	SER325
F	SER325

site_id	SWS_FT_FI10
Number of Residues	6
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
B	ASN603
C	ASN603
D	ASN603
E	ASN603
F	ASN603

site_id	SWS_FT_FI11
Number of Residues	12
Details	CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269\|PubMed:34732583

Chain	Residue	Details
A	THR676
E	THR678
F	THR676
F	THR678
A	THR678
B	THR676
B	THR678
C	THR676
C	THR678
D	THR676
D	THR678
E	THR676

site_id	SWS_FT_FI12
Number of Residues	6
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
B	ASN1134
C	ASN1134
D	ASN1134
E	ASN1134
F	ASN1134

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