2QWK
THE X-RAY STRUCTURE OF A COMPLEX OF 5-N-ACETYL-5-AMINO-3-(1-ETHYLPROPOXY)-1-CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE
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 | ASP151 | |
| A | GLU277 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a4g |
| Chain | Residue | Details |
| A | GLU277 | |
| A | ASP151 | |
| A | ARG220 | |
| A | TRP12 | |
| A | ARG371 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| A | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| A | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | ARG292 | electrostatic stabiliser |
| A | ARG371 | electrostatic stabiliser |
| A | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
