1INX
A SIALIC ACID DERIVED PHOSPHONATE ANALOG INHIBITS DIFFERENT STRAINS OF INFLUENZA VIRUS NEURAMINIDASE WITH DIFFERENT EFFICIENCIES
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 | 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 |
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 | 1 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | ASP151 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | TYR406 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | ARG118 | |
| A | ARG152 | |
| A | GLU276 | |
| A | ARG292 | |
| A | ARG371 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809 |
| Chain | Residue | Details |
| A | ASP293 | |
| A | GLY297 | |
| A | ASP324 | |
| A | GLY345 | |
| A | THR346 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809 |
| Chain | Residue | Details |
| A | GLN347 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809 |
| Chain | Residue | Details |
| A | ASN86 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000269|PubMed:1920428, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809 |
| Chain | Residue | Details |
| A | ASN146 | |
| A | ASN200 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7844831, ECO:0000269|PubMed:7880809 |
| Chain | Residue | Details |
| A | ASN234 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | ASN402 |
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 |
