Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7YR3

SARS-CoV-2 BA.2.75 S Trimer in complex with ACE2(state2)

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006508	biological_process	proteolysis
D	0008237	molecular_function	metallopeptidase activity
D	0008241	molecular_function	peptidyl-dipeptidase activity
D	0016020	cellular_component	membrane
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
G	0006508	biological_process	proteolysis
G	0008237	molecular_function	metallopeptidase activity
G	0008241	molecular_function	peptidyl-dipeptidase activity
G	0016020	cellular_component	membrane

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. TAHHEMGHIQ

Chain	Residue	Details
D	THR371-GLN380

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000305\|PubMed:14754895, ECO:0000305\|PubMed:27217402

Chain	Residue	Details
D	GLU375
G	GLU375
F	GLN17-ILE1216

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000305\|PubMed:14754895

Chain	Residue	Details
D	HIS505
G	HIS505
F	TRP1217-MET1237

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:14754895, ECO:0000305\|PubMed:19021774

Chain	Residue	Details
D	ARG169
D	TRP477
D	LYS481
G	ARG169
G	TRP477
G	LYS481

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000305\|PubMed:14754895

Chain	Residue	Details
D	ARG273
D	HIS345
D	TYR515
G	ARG273
G	HIS345
G	TYR515

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01355, ECO:0000269\|PubMed:14754895

Chain	Residue	Details
D	HIS374
D	HIS378
D	GLU402
G	HIS374
G	HIS378
G	GLU402

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305\|PubMed:14754895

Chain	Residue	Details
D	ASN53
C	GLY1246
F	THR1238
F	SER1239
F	CYS1243
F	LEU1244
F	GLY1246
D	ASN322
G	ASN53
G	ASN322
B	GLY1246
C	THR1238
C	SER1239
C	CYS1243
C	LEU1244

site_id	SWS_FT_FI7
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:14754895, ECO:0000269\|PubMed:15084671, ECO:0000269\|PubMed:19901337

Chain	Residue	Details
D	ASN90
C	ASP1257
F	CYS1250
F	GLY1251
F	CYS1253
F	PHE1256
F	ASP1257
G	ASN90
B	CYS1253
B	PHE1256
B	ASP1257
C	CYS1250
C	GLY1251
C	CYS1253
C	PHE1256

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:14754895

Chain	Residue	Details
D	ASN103
D	ASN432
G	ASN103
G	ASN432
C	SER1161
C	VAL1176
F	ASN20
F	SER1161
F	VAL1176

site_id	SWS_FT_FI9
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269\|PubMed:14754895, ECO:0000269\|PubMed:19159218, ECO:0000269\|PubMed:19901337

Chain	Residue	Details
D	ASN546
C	THR1077
F	TRP64
F	ASN125
F	ILE720
F	GLN804
F	THR1077
G	ASN546
B	ILE720
B	GLN804
B	THR1077
C	TRP64
C	ASN125
C	ILE720
C	GLN804

site_id	SWS_FT_FI10
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
B	LYS77
B	ARG152
B	LEU1197
C	LYS77
C	ARG152
C	LEU1197
F	LYS77
F	ARG152
F	LEU1197

site_id	SWS_FT_FI11
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
B	PHE168
C	ASN334
C	ARG346
C	GLU619
C	TYR660
C	HIS1101
F	PHE168
F	ILE285
F	ASN334
F	ARG346
F	GLU619
B	ILE285
F	TYR660
F	HIS1101
B	ASN334
B	ARG346
B	GLU619
B	TYR660
B	HIS1101
C	PHE168
C	ILE285

site_id	SWS_FT_FI12
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
B	ARG237
B	ILE712
C	ARG237
C	ILE712
F	ARG237
F	ILE712

site_id	SWS_FT_FI13
Number of Residues	3
Details	CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
B	ILE326
C	ILE326
F	ILE326

site_id	SWS_FT_FI14
Number of Residues	3
Details	CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269\|PubMed:32363391

Chain	Residue	Details
B	ARG328
C	ARG328
F	ARG328

site_id	SWS_FT_FI15
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
B	ASN606
C	ASN606
F	ASN606

site_id	SWS_FT_FI16
Number of Residues	6
Details	CARBOHYD: O-linked (GlcNAc...) threonine; by host GALNT1 => ECO:0000269\|PubMed:34732583

Chain	Residue	Details
B	LYS679
B	HIS681
C	LYS679
C	HIS681
F	LYS679
F	HIS681

site_id	SWS_FT_FI17
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
B	VAL1137
C	VAL1137
F	VAL1137

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