7Y1Z

S-ECD (Omicron BA.3) in complex with three PD of 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
F	0006508	biological_process	proteolysis
F	0008237	molecular_function	metallopeptidase activity
F	0008241	molecular_function	peptidyl-dipeptidase activity
F	0016020	cellular_component	membrane
H	0006508	biological_process	proteolysis
H	0008237	molecular_function	metallopeptidase activity
H	0008241	molecular_function	peptidyl-dipeptidase activity
H	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	3
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402

Chain	Residue	Details
D	GLU375
F	GLU375
H	GLU375

---

site_id	SWS_FT_FI2
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	HIS505
F	HIS505
H	HIS505

---

site_id	SWS_FT_FI3
Number of Residues	9
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
F	ARG169
F	TRP477
F	LYS481
H	ARG169
H	TRP477
H	LYS481

---

site_id	SWS_FT_FI4
Number of Residues	9
Details	BINDING: BINDING => ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	ARG273
D	HIS345
D	TYR515
F	ARG273
F	HIS345
F	TYR515
H	ARG273
H	HIS345
H	TYR515
B	ALA1080
C	ASN61
C	THR124
C	THR723
C	PRO807
C	ALA1080

---

site_id	SWS_FT_FI5
Number of Residues	9
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895

Chain	Residue	Details
D	HIS374
D	HIS378
D	GLU402
F	HIS374
F	HIS378
F	GLU402
H	HIS374
H	HIS378
H	GLU402

---

site_id	SWS_FT_FI6
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895

Chain	Residue	Details
D	ASN53
D	ASN322
F	ASN53
F	ASN322
H	ASN53
H	ASN322
A	VAL1104
B	TYR170
B	ALA288
B	PRO337
B	SER349
B	VAL622
B	ASP663
B	VAL1104
C	TYR170
C	ALA288
C	PRO337
C	SER349
C	VAL622
C	ASP663
C	VAL1104

---

site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:19901337

Chain	Residue	Details
D	ASN90
F	ASN90
H	ASN90
B	PRO715
C	THR240
C	PRO715

---

site_id	SWS_FT_FI8
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895

Chain	Residue	Details
D	ASN103
D	ASN432
F	ASN103
F	ASN432
H	ASN103
H	ASN432

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337

Chain	Residue	Details
D	ASN546
F	ASN546
H	ASN546

---

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	ALA609
B	ALA609
C	ALA609

---

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	GLY682
A	ALA684
B	GLY682
B	ALA684
C	GLY682
C	ALA684

---

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	PRO1140
B	PRO1140
C	PRO1140

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