7WPA

SARS-CoV-2 Omicron Variant SPIKE trimer complexed with ACE2

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	0006508	biological_process	proteolysis
D	0008237	molecular_function	metallopeptidase activity
D	0008241	molecular_function	peptidyl-dipeptidase activity
D	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

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	722
Details	TOPO_DOM: Extracellular => ECO:0000255

Chain	Residue	Details
D	GLN18-SER740
B	SER682
C	SER682

---

site_id	SWS_FT_FI2
Number of Residues	20
Details	TRANSMEM: Helical => ECO:0000255|PROSITE-ProRule:PRU01354

Chain	Residue	Details
D	ILE741-ILE761
B	ARG812
C	ARG812

---

site_id	SWS_FT_FI3
Number of Residues	43
Details	TOPO_DOM: Cytoplasmic => ECO:0000255

Chain	Residue	Details
D	PHE762-PHE805
A	ASN1155
A	ASN1170
B	ASN17
B	ASN1155
B	ASN1170
C	ASN17
C	ASN1155
C	ASN1170

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402

Chain	Residue	Details
D	GLU375
B	ASN1071
C	ASN61
C	THR122
C	ASN714
C	ASN798
C	ASN1071
A	THR122
A	ASN714
A	ASN798
A	ASN1071
B	ASN61
B	THR122
B	ASN714
B	ASN798

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	HIS505
A	GLU149
A	ASN1191
B	THR74
B	GLU149
B	ASN1191
C	THR74
C	GLU149
C	ASN1191

---

site_id	SWS_FT_FI6
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774

Chain	Residue	Details
D	ARG169
B	ASN328
B	ASN340
B	ASN613
B	ASN654
B	ASN1095
C	TYR165
C	ASN279
C	ASN328
C	ASN340
C	ASN613
D	TRP477
C	ASN654
C	ASN1095
D	LYS481
A	ASN340
A	ASN613
A	ASN654
A	ASN1095
B	TYR165
B	ASN279

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	ARG273
D	HIS345
D	TYR515
B	ASN706
C	ASN231
C	ASN706

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895

Chain	Residue	Details
D	HIS374
D	HIS378
D	GLU402

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498

Chain	Residue	Details
D	TYR781
B	SER322
C	SER322

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000305|PubMed:33436497, ECO:0000305|PubMed:33436498

Chain	Residue	Details
D	SER783
B	ASN600
C	ASN600

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	ASN53
D	ASN322
B	THR673
B	THR675
C	THR673
C	THR675

---

site_id	SWS_FT_FI12
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337

Chain	Residue	Details
D	ASN90
B	ASN1131
C	ASN1131

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895

Chain	Residue	Details
D	ASN103
D	ASN432

---

site_id	SWS_FT_FI14
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337

Chain	Residue	Details
D	ASN546

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site_id	SWS_FT_FI15
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
D	ASN690

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site_id	SWS_FT_FI16
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:36876523

Chain	Residue	Details
D	LYS788

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