6LXI
Crystal structure of Z2B3 Fab in complex with influenza virus neuraminidase from A/Brevig Mission/1/1918 (H1N1)
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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0020002 | cellular_component | host cell plasma membrane |
| A | 0033644 | cellular_component | host cell membrane |
| A | 0044423 | cellular_component | virion component |
| A | 0046761 | biological_process | viral budding from plasma membrane |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0020002 | cellular_component | host cell plasma membrane |
| B | 0033644 | cellular_component | host cell membrane |
| B | 0044423 | cellular_component | virion component |
| B | 0046761 | biological_process | viral budding from plasma membrane |
| B | 0046872 | molecular_function | metal ion binding |
| B | 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. YICNVNH |
| Chain | Residue | Details |
| H | TYR213-HIS219 | |
| L | TYR195-HIS201 |
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 | 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_FI3 |
| 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_FI4 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18715929","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine; by host","evidences":[{"source":"HAMAP-Rule","id":"MF_04071","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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":"18715929","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
