1XOG
N9 Tern Influenza neuraminidase complexed with a 2,5-Disubstituted tetrahydrofuran-5-carboxylic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0004308 | molecular_function | exo-alpha-sialidase activity | 
| A | 0005975 | biological_process | carbohydrate metabolic process | 
| A | 0016020 | cellular_component | membrane | 
| A | 0033644 | cellular_component | host cell membrane | 
| A | 0046761 | biological_process | viral budding from plasma membrane | 
| A | 0055036 | cellular_component | virion membrane | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 378 | 
| Details | Region: {"description":"Head of neuraminidase","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 1 | 
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 1 | 
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 5 | 
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 4 | 
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23429702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7549872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8371267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342319","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 3 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23429702","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7549872","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9342319","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1a4g | 
| Chain | Residue | Details | 
| A | ASP152 | |
| A | GLU279 | 
| site_id | MCSA1 | 
| Number of Residues | 5 | 
| Details | M-CSA 828 | 
| Chain | Residue | Details | 
| A | ASP152 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor | 
| A | GLU279 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor | 
| A | ARG294 | electrostatic stabiliser | 
| A | ARG372 | electrostatic stabiliser | 
| A | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor | 






