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 | 10 |
Details | TOPO_DOM: Intravirion => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | MET1-LYS6 | |
B | MET1-LYS6 |
site_id | SWS_FT_FI2 |
Number of Residues | 40 |
Details | TRANSMEM: Helical => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ILE7-GLY27 | |
B | ILE7-GLY27 |
site_id | SWS_FT_FI3 |
Number of Residues | 882 |
Details | TOPO_DOM: Virion surface => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ASN28-LYS469 | |
B | ASN28-LYS469 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ASP151 | |
B | ASP151 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | TYR402 | |
B | TYR402 |
site_id | SWS_FT_FI6 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ARG118 | |
B | ARG368 | |
A | ARG152 | |
A | GLU277 | |
A | ARG293 | |
A | ARG368 | |
B | ARG118 | |
B | ARG152 | |
B | GLU277 | |
B | ARG293 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929 |
Chain | Residue | Details |
A | ASP294 | |
A | GLY298 | |
A | ASP324 | |
A | ASN344 | |
B | ASP294 | |
B | GLY298 | |
B | ASP324 | |
B | ASN344 |
site_id | SWS_FT_FI8 |
Number of Residues | 12 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ASN50 | |
B | ASN68 | |
B | ASN88 | |
B | ASN235 | |
A | ASN58 | |
A | ASN63 | |
A | ASN68 | |
A | ASN88 | |
A | ASN235 | |
B | ASN50 | |
B | ASN58 | |
B | ASN63 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:18715929 |
Chain | Residue | Details |
A | ASN146 | |
B | ASN146 |