1IVE
STRUCTURES OF AROMATIC INHIBITORS OF 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 |
| B | 0004308 | molecular_function | exo-alpha-sialidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0033644 | cellular_component | host cell membrane |
| B | 0046761 | biological_process | viral budding from plasma membrane |
| B | 0055036 | cellular_component | virion membrane |
Functional Information from PDB Data
| site_id | CAT |
| Number of Residues | 11 |
| Details | SUBSTRATE (SIALIC ACID) BINDING RESIDUES IN CATALYTIC SITE |
| Chain | Residue |
| A | ARG118 |
| A | ARG371 |
| A | TYR406 |
| A | GLU119 |
| A | ASP151 |
| A | ARG152 |
| A | TRP178 |
| A | ILE222 |
| A | ARG224 |
| A | GLU276 |
| A | ARG292 |
| site_id | CT2 |
| Number of Residues | 11 |
| Details |
| Chain | Residue |
| B | ARG118 |
| B | GLU119 |
| B | ASP151 |
| B | ARG152 |
| B | TRP178 |
| B | ILE222 |
| B | ARG224 |
| B | GLU276 |
| B | ARG292 |
| B | ARG371 |
| B | TYR406 |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CsCypRypGVrC |
| Chain | Residue | Details |
| A | CYS278-CYS289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 756 |
| 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 | 50 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Compositional bias: {"description":"Low complexity","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1920428","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7844831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7880809","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1920428","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7844831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7880809","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1920428","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7844831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7880809","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"PubMed","id":"1920428","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7844831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7880809","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7844831","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7880809","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1a4g |
| Chain | Residue | Details |
| B | ASP151 | |
| B | GLU277 |
