1NMB
THE STRUCTURE OF A COMPLEX BETWEEN THE NC10 ANTIBODY AND INFLUENZA VIRUS NEURAMINIDASE AND COMPARISON WITH THE OVERLAPPING BINDING SITE OF THE NC41 ANTIBODY
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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| N | 0020002 | cellular_component | host cell plasma membrane |
| N | 0033644 | cellular_component | host cell membrane |
| N | 0044423 | cellular_component | virion component |
| N | 0046761 | biological_process | viral budding from plasma membrane |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0052794 | molecular_function | exo-alpha-(2->3)-sialidase activity |
| N | 0052795 | molecular_function | exo-alpha-(2->6)-sialidase activity |
| N | 0052796 | molecular_function | exo-alpha-(2->8)-sialidase activity |
| N | 0055036 | cellular_component | virion membrane |
Functional Information from PROSITE/UniProt
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CsCygEqaGVtC |
| Chain | Residue | Details |
| N | CYS278-CYS289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 13 |
| Details | TOPO_DOM: Intravirion => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| N | MET0-ALA13 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| N | LEU14-LEU34 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 434 |
| Details | TOPO_DOM: Virion surface => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| N | HIS35-LEU468 |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| N | TYR406 |
| site_id | SWS_FT_FI6 |
| 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_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7994573 |
| Chain | Residue | Details |
| N | ASP293 | |
| N | GLY297 | |
| N | ASP324 | |
| N | ASN347 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 5 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| N | ASN41 | |
| N | ASN51 | |
| N | ASN62 | |
| N | ASN65 | |
| N | ASN200 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7517697, ECO:0000269|PubMed:7994573 |
| Chain | Residue | Details |
| N | ASN86 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7994573 |
| Chain | Residue | Details |
| N | ASN146 |
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 |
