1NNA
THREE-DIMENSIONAL STRUCTURE OF INFLUENZA A N9 NEURAMINIDASE AND ITS COMPLEX WITH THE INHIBITOR 2-DEOXY 2,3-DEHYDRO-N-ACETYL NEURAMINIC 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 PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 471 |
| Chain | Residue |
| A | ASP295 |
| A | GLY299 |
| A | ASP326 |
| A | ASN348 |
| site_id | CAL |
| Number of Residues | 4 |
| Details |
| Chain | Residue |
| A | ASP295 |
| A | GLY299 |
| A | ASP326 |
| A | GLY349 |
| site_id | SUB |
| Number of Residues | 18 |
| Details |
| Chain | Residue |
| A | ARG119 |
| A | HIS276 |
| A | GLU278 |
| A | GLU279 |
| A | ARG294 |
| A | ASN296 |
| A | GLY349 |
| A | ARG372 |
| A | TYR406 |
| A | GLU427 |
| A | GLU120 |
| A | ASP152 |
| A | ARG153 |
| A | TRP180 |
| A | SER181 |
| A | ILE224 |
| A | ARG226 |
| A | GLU229 |
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 |
