6APD

Crystal structure of RSV F bound by AM22 and the infant antibody ADI-19425

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0019064	biological_process	fusion of virus membrane with host plasma membrane
B	0019064	biological_process	fusion of virus membrane with host plasma membrane
C	0019064	biological_process	fusion of virus membrane with host plasma membrane
E	0005576	cellular_component	extracellular region
E	0046872	molecular_function	metal ion binding
G	0005576	cellular_component	extracellular region
G	0046872	molecular_function	metal ion binding
I	0005576	cellular_component	extracellular region
I	0046872	molecular_function	metal ion binding
J	0002250	biological_process	adaptive immune response
J	0003823	molecular_function	antigen binding
J	0005576	cellular_component	extracellular region
J	0005886	cellular_component	plasma membrane
J	0016064	biological_process	immunoglobulin mediated immune response
J	0019814	cellular_component	immunoglobulin complex
K	0002250	biological_process	adaptive immune response
K	0003823	molecular_function	antigen binding
K	0005576	cellular_component	extracellular region
K	0005886	cellular_component	plasma membrane
K	0016064	biological_process	immunoglobulin mediated immune response
K	0019814	cellular_component	immunoglobulin complex
N	0002250	biological_process	adaptive immune response
N	0003823	molecular_function	antigen binding
N	0005576	cellular_component	extracellular region
N	0005886	cellular_component	plasma membrane
N	0016064	biological_process	immunoglobulin mediated immune response
N	0019814	cellular_component	immunoglobulin complex

Functional Information from PROSITE/UniProt

site_id	PS00290
Number of Residues	7
Details	IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH

Chain	Residue	Details
J	TYR194-HIS200
L	TYR192-HIS198
E	TYR192-HIS198
D	TYR194-HIS200

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	SITE: Cleavage; by host furin-like protease => ECO:0000269|PubMed:11493675, ECO:0000269|PubMed:12127793

Chain	Residue	Details
A	ARG109
B	ARG109
C	ARG109

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site_id	SWS_FT_FI2
Number of Residues	3
Details	SITE: Cleavage; by host furin-like protease => ECO:0000269|PubMed:11369882, ECO:0000269|PubMed:12127793

Chain	Residue	Details
A	ARG136
B	ARG136
C	ARG136

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site_id	SWS_FT_FI3
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:21586636

Chain	Residue	Details
A	ASN27
B	ASN27
C	ASN27

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site_id	SWS_FT_FI4
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:21586636, ECO:0000269|PubMed:28469033

Chain	Residue	Details
A	ASN70
B	ASN70
C	ASN70

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site_id	SWS_FT_FI5
Number of Residues	9
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255

Chain	Residue	Details
A	ASN116
A	ASN120
A	ASN126
B	ASN116
B	ASN120
B	ASN126
C	ASN116
C	ASN120
C	ASN126

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site_id	SWS_FT_FI6
Number of Residues	3
Details	CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:21586636, ECO:0000269|PubMed:24179220

Chain	Residue	Details
A	ASN500
B	ASN500
C	ASN500

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