9MV0

Structure of HKU5 spike C-terminal domain in complex with ACE2 from Pipistrellus abramus

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008241	molecular_function	peptidyl-dipeptidase activity
A	0016020	cellular_component	membrane
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	0006508	biological_process	proteolysis
C	0008237	molecular_function	metallopeptidase activity
C	0008241	molecular_function	peptidyl-dipeptidase activity
C	0016020	cellular_component	membrane
D	0016020	cellular_component	membrane
D	0019031	cellular_component	viral envelope
D	0019064	biological_process	fusion of virus membrane with host plasma membrane
D	0039654	biological_process	fusion of virus membrane with host endosome membrane
D	0046813	biological_process	receptor-mediated virion attachment to host cell
D	0055036	cellular_component	virion membrane
D	0075509	biological_process	endocytosis involved in viral entry into host cell

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
A	THR370-GLN379

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI10
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04099","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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