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6HCX

Influenza Virus N9 Neuraminidase A complex with Zanamivir molecule (Tern).

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005975biological_processcarbohydrate metabolic process
A0016020cellular_componentmembrane
A0033644cellular_componenthost cell membrane
A0046761biological_processviral budding from plasma membrane
A0055036cellular_componentvirion membrane
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AASP152

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
ATYR406

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071
ChainResidueDetails
AARG119
AARG153
AGLU278
AARG294
AARG372

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319
ChainResidueDetails
AASP295
AGLY299
AASP326
AASN348

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319
ChainResidueDetails
AASN87
AASN147
AASN202

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 828
ChainResidueDetails
AASP152activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor
AGLU279activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AARG294electrostatic stabiliser
AARG372electrostatic stabiliser
ATYR406electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor

217705

PDB entries from 2024-03-27

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