7SXX

Cryo-EM structure of the SARS-CoV-2 D614G mutant spike protein ectodomain bound to human ACE2 ectodomain (global refinement)

This is a non-PDB format compatible entry.

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
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
E	THR371-GLN380

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895, ECO:0000305|PubMed:27217402

Chain	Residue	Details
C	SER685
E	GLU375
B	SER685

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000305|PubMed:14754895

Chain	Residue	Details
C	ARG815
E	HIS505
B	ARG815

---

site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895, ECO:0000305|PubMed:19021774

Chain	Residue	Details
C	ASN17
C	ASN1158
C	ASN1173
E	ARG169
E	TRP477
E	LYS481
B	ASN17
B	ASN1158
B	ASN1173

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:14754895

Chain	Residue	Details
B	ASN801
B	ASN1074
C	ASN61
C	ASN122
C	ASN717
C	ASN801
C	ASN1074
E	ARG273
E	HIS345
E	TYR515
A	ASN801
A	ASN1074
B	ASN61
B	ASN122
B	ASN717

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01355, ECO:0000269|PubMed:14754895

Chain	Residue	Details
C	ASN74
C	ASN149
C	ASN1194
B	ASN74
B	ASN149
B	ASN1194
E	GLU402
E	HIS374
E	HIS378

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305|PubMed:14754895

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

---

site_id	SWS_FT_FI7
Number of Residues	1
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
A	ASN709
B	ASN234
E	ASN90

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895

Chain	Residue	Details
E	ASN103
E	ASN432
C	THR323

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:14754895, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19901337

Chain	Residue	Details
E	ASN546
B	SER325
C	SER325

---

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

---

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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