8DM7

Cryo-EM structure of SARS-CoV-2 Omicron BA.2 spike protein in complex with mouse 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

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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site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. ATSTdyNsRLWAWEG

Chain	Residue	Details
D	ALA153-GLY167

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	GLU375
E	GLU375
C	ALA688

---

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

Chain	Residue	Details
D	HIS505
E	HIS505
C	ILE818

---

site_id	SWS_FT_FI3
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	ARG169
E	GLU402
E	TRP477
E	LYS481
D	HIS374
D	HIS378
D	GLU402
D	TRP477
D	LYS481
E	ARG169
E	HIS374
E	HIS378

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1

Chain	Residue	Details
D	ARG273
B	THR1077
C	TRP64
C	ASN125
C	ILE720
C	GLN804
C	THR1077
D	HIS345
D	TYR515
E	ARG273
E	HIS345
E	TYR515
B	ASN125
B	ILE720
B	GLN804

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
D	ASN53
D	ASN536
D	ASN546
E	ASN53
E	ASN536
E	ASN546
C	LYS77
C	TRP152
C	LEU1197

---

site_id	SWS_FT_FI6
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
A	PHE168
B	ASN334
B	ARG346
B	GLU619
B	TYR660
B	HIS1101
C	PHE168
C	ILE285
C	ASN334
C	ARG346
C	GLU619
A	ILE285
C	TYR660
C	HIS1101
A	ASN334
A	ARG346
A	GLU619
A	TYR660
A	HIS1101
B	PHE168
B	ILE285

---

site_id	SWS_FT_FI7
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
A	ARG237
A	ILE712
B	ARG237
B	ILE712
C	ARG237
C	ILE712

---

site_id	SWS_FT_FI8
Number of Residues	3
Details	CARBOHYD: O-linked (GalNAc) threonine; by host => ECO:0000269|PubMed:32363391

Chain	Residue	Details
A	ILE326
B	ILE326
C	ILE326

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: O-linked (HexNAc...) serine; by host => ECO:0000269|PubMed:32363391

Chain	Residue	Details
A	ARG328
B	ARG328
C	ARG328

---

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	ASN606
B	ASN606
C	ASN606

---

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	LYS679
A	HIS681
B	LYS679
B	HIS681
C	LYS679
C	HIS681

---

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	VAL1137
B	VAL1137
C	VAL1137

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