8VKM

Cryo-EM structure of SARS-CoV-2 XBB.1.5 spike protein in complex with mouse ACE2 (conformation 1)

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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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	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	GLU375
B	SER689
C	SER689

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	HIS505
B	GLU819
C	GLU819

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site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355

Chain	Residue	Details
D	ARG169
D	HIS374
D	HIS378
D	GLU402
D	TRP477
D	LYS481
C	ASN17
C	PRO1162
C	VAL1177

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site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q9BYF1

Chain	Residue	Details
D	ARG273
B	ALA1078
C	TRP64
C	ASN125
C	SER721
C	ILE805
C	ALA1078
D	HIS345
D	TYR515
A	ILE805
A	ALA1078
B	TRP64
B	ASN125
B	SER721
B	ILE805

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
D	ASN53
D	ASN536
D	ASN546
B	LYS77
B	MET153
B	ILE1198
C	LYS77
C	MET153
C	ILE1198

---

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	GLU169
B	LEU335
B	PHE347
B	VAL620
B	GLU661
B	TRP1102
C	GLU169
C	THR286
C	LEU335
C	PHE347
C	VAL620
A	THR286
C	GLU661
C	TRP1102
A	LEU335
A	PHE347
A	VAL620
A	GLU661
A	TRP1102
B	GLU169
B	THR286

---

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	PHE238
A	ALA713
B	PHE238
B	ALA713
C	PHE238
C	ALA713

---

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	VAL327
B	VAL327
C	VAL327

---

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	PHE329
B	PHE329
C	PHE329

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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	GLN607
B	GLN607
C	GLN607

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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	SER680
A	GLY682
B	SER680
B	GLY682
C	SER680
C	GLY682

---

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	TYR1138
B	TYR1138
C	TYR1138

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