Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7V82

Cryo-EM structure of SARS-CoV-2 S-Gamma variant (P.1) in complex with Angiotensin-converting enzyme 2 (ACE2) ectodomain, three ACE2-bound form 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	0006091	biological_process	generation of precursor metabolites and energy
D	0006508	biological_process	proteolysis
D	0008218	biological_process	bioluminescence
D	0008237	molecular_function	metallopeptidase activity
D	0008241	molecular_function	peptidyl-dipeptidase activity
D	0016020	cellular_component	membrane
E	0006091	biological_process	generation of precursor metabolites and energy
E	0006508	biological_process	proteolysis
E	0008218	biological_process	bioluminescence
E	0008237	molecular_function	metallopeptidase activity
E	0008241	molecular_function	peptidyl-dipeptidase activity
E	0016020	cellular_component	membrane
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

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
E	THR371-GLN380

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
E	GLU375
D	GLU375
F	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
E	HIS505
D	HIS505
F	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
E	ARG169
E	TRP477
E	LYS481
D	ARG169
D	TRP477
D	LYS481
F	ARG169
F	TRP477
F	LYS481

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

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

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

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

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
E	ASN90
D	ASN90
F	ASN90
B	ASN709
C	ASN234
C	ASN709

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

Chain	Residue	Details
E	ASN103
E	ASN432
D	ASN103
D	ASN432
F	ASN103
F	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
E	ASN546
D	ASN546
F	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

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	THR676
A	THR678
B	THR676
B	THR678
C	THR676
C	THR678

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

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)