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1FLC

X-RAY STRUCTURE OF THE HAEMAGGLUTININ-ESTERASE-FUSION GLYCOPROTEIN OF INFLUENZA C VIRUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0016788molecular_functionhydrolase activity, acting on ester bonds
A0019031cellular_componentviral envelope
A0019064biological_processfusion of virus membrane with host plasma membrane
A0046789molecular_functionhost cell surface receptor binding
B0019031cellular_componentviral envelope
B0019064biological_processfusion of virus membrane with host plasma membrane
B0046789molecular_functionhost cell surface receptor binding
C0016788molecular_functionhydrolase activity, acting on ester bonds
C0019031cellular_componentviral envelope
C0019064biological_processfusion of virus membrane with host plasma membrane
C0046789molecular_functionhost cell surface receptor binding
D0019031cellular_componentviral envelope
D0019064biological_processfusion of virus membrane with host plasma membrane
D0046789molecular_functionhost cell surface receptor binding
E0016788molecular_functionhydrolase activity, acting on ester bonds
E0019031cellular_componentviral envelope
E0019064biological_processfusion of virus membrane with host plasma membrane
E0046789molecular_functionhost cell surface receptor binding
F0019031cellular_componentviral envelope
F0019064biological_processfusion of virus membrane with host plasma membrane
F0046789molecular_functionhost cell surface receptor binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues75
DetailsRegion: {"description":"Fusion domain-1","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues351
DetailsRegion: {"description":"Esterase domain-1","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues330
DetailsRegion: {"description":"Esterase domain-1"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues477
DetailsRegion: {"description":"N-acetyl-9-O-acetylneuraminic acid binding"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues456
DetailsRegion: {"description":"N-acetyl-9-O-acetylneuraminic acid binding","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues162
DetailsRegion: {"description":"Esterase domain-2","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues162
DetailsRegion: {"description":"Esterase domain-2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues6
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues21
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04072","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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