8I9C

S-ECD (Omicron BF.7) in complex with 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
E	0006508	biological_process	proteolysis
E	0008237	molecular_function	metallopeptidase activity
E	0008241	molecular_function	peptidyl-dipeptidase activity
E	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

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
F	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
F	GLU375
D	GLU375
E	GLU375

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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
F	HIS505
D	HIS505
E	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
F	ARG169
F	TRP477
F	LYS481
D	ARG169
D	TRP477
D	LYS481
E	ARG169
E	TRP477
E	LYS481

---

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

Chain	Residue	Details
F	ARG273
B	PRO1079
C	TRP64
C	VAL127
C	VAL722
C	LEU806
C	PRO1079
F	HIS345
F	TYR515
D	ARG273
D	HIS345
D	TYR515
E	ARG273
E	HIS345
E	TYR515

---

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

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

---

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

Chain	Residue	Details
F	ASN53
B	CYS336
B	ALA348
B	PRO621
B	CYS662
B	PHE1103
C	TYR170
C	ASP287
C	CYS336
C	ALA348
C	PRO621
F	ASN322
C	CYS662
C	PHE1103
D	ASN53
D	ASN322
E	ASN53
E	ASN322
A	PHE1103
B	TYR170
B	ASP287

---

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
F	ASN90
D	ASN90
E	ASN90
B	ILE714
C	GLN239
C	ILE714

---

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

Chain	Residue	Details
F	ASN103
F	ASN432
D	ASN103
D	ASN432
E	ASN103
E	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
F	ASN546
D	ASN546
E	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	VAL608
B	VAL608
C	VAL608

---

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	HIS681
A	SER683
B	HIS681
B	SER683
C	HIS681
C	SER683

---

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	ASP1139
B	ASP1139
C	ASP1139

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