1NCA
REFINED CRYSTAL STRUCTURE OF THE INFLUENZA VIRUS N9 NEURAMINIDASE-NC41 FAB COMPLEX
Functional Information from GO Data
Chain | GOid | namespace | contents |
N | 0004308 | molecular_function | exo-alpha-sialidase activity |
N | 0005975 | biological_process | carbohydrate metabolic process |
N | 0016020 | cellular_component | membrane |
N | 0033644 | cellular_component | host cell membrane |
N | 0046761 | biological_process | viral budding from plasma membrane |
N | 0055036 | cellular_component | virion membrane |
Functional Information from PROSITE/UniProt
site_id | PS00290 |
Number of Residues | 7 |
Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH |
Chain | Residue | Details |
L | TYR192-HIS198 |
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 |
N | ASP151 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
N | TYR406 |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
N | ARG118 | |
N | ARG152 | |
N | GLU276 | |
N | ARG292 | |
N | ARG371 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:8371267, ECO:0000269|PubMed:9342319 |
Chain | Residue | Details |
N | ASP293 | |
N | GLY297 | |
N | ASP324 | |
N | ASN347 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:23429702, ECO:0000269|PubMed:7549872, ECO:0000269|PubMed:9342319 |
Chain | Residue | Details |
N | ASN86 | |
N | ASN146 | |
N | ASN200 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
N | ASP151 | |
N | GLU277 |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
N | GLU277 | |
N | ASP151 | |
N | ARG220 | |
N | TRP412 | |
N | ARG371 |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 828 |
Chain | Residue | Details |
N | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
N | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
N | ARG292 | electrostatic stabiliser |
N | ARG371 | electrostatic stabiliser |
N | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |