3MQ7

Crystal Structure of Ectodomain Mutant of BST-2/Tetherin/CD317

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0051607	biological_process	defense response to virus
B	0051607	biological_process	defense response to virus
C	0051607	biological_process	defense response to virus
D	0051607	biological_process	defense response to virus
E	0051607	biological_process	defense response to virus
F	0051607	biological_process	defense response to virus
G	0051607	biological_process	defense response to virus
H	0051607	biological_process	defense response to virus
I	0051607	biological_process	defense response to virus
J	0051607	biological_process	defense response to virus
K	0051607	biological_process	defense response to virus
L	0051607	biological_process	defense response to virus

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA E 1

Chain	Residue
E	HOH34
E	GLU73
E	GLU76
E	HOH164
E	HOH166

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CA K 1

Chain	Residue
K	HOH26
K	GLU73
K	GLU76

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19737401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19879838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19737401","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19879838","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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