7VPQ

Structures of a deltacoronavirus spike protein bound to porcine and human receptors indicate the risk of virus adaptation to humans

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0001618	molecular_function	virus receptor activity
A	0004177	molecular_function	aminopeptidase activity
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
A	0005886	cellular_component	plasma membrane
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009897	cellular_component	external side of plasma membrane
A	0030154	biological_process	cell differentiation
A	0030667	cellular_component	secretory granule membrane
A	0038023	molecular_function	signaling receptor activity
A	0042277	molecular_function	peptide binding
A	0043171	biological_process	peptide catabolic process
A	0046718	biological_process	symbiont entry into host cell
A	0046872	molecular_function	metal ion binding
A	0070006	molecular_function	metalloaminopeptidase activity
A	0070062	cellular_component	extracellular exosome
B	0019064	biological_process	fusion of virus membrane with host plasma membrane
C	0001525	biological_process	angiogenesis
C	0001618	molecular_function	virus receptor activity
C	0004177	molecular_function	aminopeptidase activity
C	0005615	cellular_component	extracellular space
C	0005737	cellular_component	cytoplasm
C	0005765	cellular_component	lysosomal membrane
C	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
C	0005886	cellular_component	plasma membrane
C	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008270	molecular_function	zinc ion binding
C	0009897	cellular_component	external side of plasma membrane
C	0030154	biological_process	cell differentiation
C	0030667	cellular_component	secretory granule membrane
C	0038023	molecular_function	signaling receptor activity
C	0042277	molecular_function	peptide binding
C	0043171	biological_process	peptide catabolic process
C	0046718	biological_process	symbiont entry into host cell
C	0046872	molecular_function	metal ion binding
C	0070006	molecular_function	metalloaminopeptidase activity
C	0070062	cellular_component	extracellular exosome
D	0019064	biological_process	fusion of virus membrane with host plasma membrane
E	0001525	biological_process	angiogenesis
E	0001618	molecular_function	virus receptor activity
E	0004177	molecular_function	aminopeptidase activity
E	0005615	cellular_component	extracellular space
E	0005737	cellular_component	cytoplasm
E	0005765	cellular_component	lysosomal membrane
E	0005793	cellular_component	endoplasmic reticulum-Golgi intermediate compartment
E	0005886	cellular_component	plasma membrane
E	0006508	biological_process	proteolysis
E	0008237	molecular_function	metallopeptidase activity
E	0008270	molecular_function	zinc ion binding
E	0009897	cellular_component	external side of plasma membrane
E	0030154	biological_process	cell differentiation
E	0030667	cellular_component	secretory granule membrane
E	0038023	molecular_function	signaling receptor activity
E	0042277	molecular_function	peptide binding
E	0043171	biological_process	peptide catabolic process
E	0046718	biological_process	symbiont entry into host cell
E	0046872	molecular_function	metal ion binding
E	0070006	molecular_function	metalloaminopeptidase activity
E	0070062	cellular_component	extracellular exosome
F	0019064	biological_process	fusion of virus membrane with host plasma membrane

Functional Information from PROSITE/UniProt

site_id	PS00142
Number of Residues	10
Details	ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIAHELAHQW

Chain	Residue	Details
A	VAL385-TRP394

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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:PRU10095, ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	GLU389
C	GLU389
E	GLU389

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	GLY352
C	GLY352
E	GLY352

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site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:22932899, ECO:0007744|PDB:4FYQ, ECO:0007744|PDB:4FYR, ECO:0007744|PDB:4FYT

Chain	Residue	Details
A	HIS388
A	HIS392
A	GLU411
C	HIS388
C	HIS392
C	GLU411
E	HIS388
E	HIS392
E	GLU411

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site_id	SWS_FT_FI4
Number of Residues	3
Details	SITE: Transition state stabilizer => ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	TYR477
C	TYR477
E	TYR477

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site_id	SWS_FT_FI5
Number of Residues	12
Details	MOD_RES: Sulfotyrosine => ECO:0000255

Chain	Residue	Details
A	TYR176
E	TYR419
E	TYR424
E	TYR913
A	TYR419
A	TYR424
A	TYR913
C	TYR176
C	TYR419
C	TYR424
C	TYR913
E	TYR176

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site_id	SWS_FT_FI6
Number of Residues	12
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	ASN128
E	ASN234
E	ASN681
E	ASN818
A	ASN234
A	ASN681
A	ASN818
C	ASN128
C	ASN234
C	ASN681
C	ASN818
E	ASN128

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site_id	SWS_FT_FI7
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15084671, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	ASN265
C	ASN265
E	ASN265

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site_id	SWS_FT_FI8
Number of Residues	9
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22932899

Chain	Residue	Details
A	ASN319
A	ASN527
A	ASN625
C	ASN319
C	ASN527
C	ASN625
E	ASN319
E	ASN527
E	ASN625

---

site_id	SWS_FT_FI9
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218

Chain	Residue	Details
A	ASN573
C	ASN573
E	ASN573

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site_id	SWS_FT_FI10
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine

Chain	Residue	Details
A	ASN735
C	ASN735
E	ASN735

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