7V86

Cryo-EM structure of SARS-CoV-2 S-Kappa variant (B.1.617.1) in complex with Angiotensin-converting enzyme 2 (ACE2) ectodomain, three ACE2-bound form

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
F	0006091	biological_process	generation of precursor metabolites and energy
F	0006508	biological_process	proteolysis
F	0008218	biological_process	bioluminescence
F	0008237	molecular_function	metallopeptidase activity
F	0008241	molecular_function	peptidyl-dipeptidase activity
F	0016020	cellular_component	membrane
G	0006091	biological_process	generation of precursor metabolites and energy
G	0006508	biological_process	proteolysis
G	0008218	biological_process	bioluminescence
G	0008237	molecular_function	metallopeptidase activity
G	0008241	molecular_function	peptidyl-dipeptidase activity
G	0016020	cellular_component	membrane
H	0006091	biological_process	generation of precursor metabolites and energy
H	0006508	biological_process	proteolysis
H	0008218	biological_process	bioluminescence
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
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
H	GLU375
F	GLU375
G	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
H	HIS505
F	HIS505
G	HIS505

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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
G	ARG169
G	TRP477
G	LYS481
H	ARG169
H	TRP477
H	LYS481

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

Chain	Residue	Details
B	ASN1074
C	ASN61
C	ASN122
C	ASN717
C	ASN801
C	ASN1074
F	ARG273
F	HIS345
F	TYR515
G	ARG273
G	HIS345
G	TYR515
H	ARG273
H	HIS345
H	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
G	GLU402
G	HIS378
H	HIS374
H	HIS378
H	GLU402
F	HIS374
F	HIS378
F	GLU402
G	HIS374

---

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

Chain	Residue	Details
C	ASN616
C	ASN657
C	ASN1098
F	ASN322
G	ASN53
G	ASN322
H	ASN53
H	ASN322
A	ASN1098
B	ASN165
B	ASN282
B	ASN331
B	ASN343
B	ASN616
B	ASN657
B	ASN1098
C	ASN165
C	ASN282
C	ASN331
C	ASN343
F	ASN53

---

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
B	ASN709
C	ASN234
C	ASN709
F	ASN90
G	ASN90
H	ASN90

---

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
G	ASN103
G	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
F	ASN546
G	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	ASN603
B	ASN603
C	ASN603

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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
B	THR678
C	THR676
C	THR678
A	THR676
A	THR678
B	THR676

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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	ASN1134
B	ASN1134
C	ASN1134

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