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 |