6CRD
INFLUENZA VIRUS NEURAMINIDASE SUBTYPE N9 (TERN) with tetrabrachion (TB) domain stalk
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 |
| B | 0004308 | molecular_function | exo-alpha-sialidase activity |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0016020 | cellular_component | membrane |
| B | 0033644 | cellular_component | host cell membrane |
| B | 0046761 | biological_process | viral budding from plasma membrane |
| B | 0055036 | cellular_component | virion membrane |
| C | 0004308 | molecular_function | exo-alpha-sialidase activity |
| C | 0005975 | biological_process | carbohydrate metabolic process |
| C | 0016020 | cellular_component | membrane |
| C | 0033644 | cellular_component | host cell membrane |
| C | 0046761 | biological_process | viral budding from plasma membrane |
| C | 0055036 | cellular_component | virion membrane |
| D | 0004308 | molecular_function | exo-alpha-sialidase activity |
| D | 0005975 | biological_process | carbohydrate metabolic process |
| D | 0016020 | cellular_component | membrane |
| D | 0033644 | cellular_component | host cell membrane |
| D | 0046761 | biological_process | viral budding from plasma membrane |
| D | 0055036 | cellular_component | virion membrane |
| E | 0004308 | molecular_function | exo-alpha-sialidase activity |
| E | 0005975 | biological_process | carbohydrate metabolic process |
| E | 0016020 | cellular_component | membrane |
| E | 0033644 | cellular_component | host cell membrane |
| E | 0046761 | biological_process | viral budding from plasma membrane |
| E | 0055036 | cellular_component | virion membrane |
| F | 0004308 | molecular_function | exo-alpha-sialidase activity |
| F | 0005975 | biological_process | carbohydrate metabolic process |
| F | 0016020 | cellular_component | membrane |
| F | 0033644 | cellular_component | host cell membrane |
| F | 0046761 | biological_process | viral budding from plasma membrane |
| F | 0055036 | cellular_component | virion membrane |
| G | 0004308 | molecular_function | exo-alpha-sialidase activity |
| G | 0005975 | biological_process | carbohydrate metabolic process |
| G | 0016020 | cellular_component | membrane |
| G | 0033644 | cellular_component | host cell membrane |
| G | 0046761 | biological_process | viral budding from plasma membrane |
| G | 0055036 | cellular_component | virion membrane |
| H | 0004308 | molecular_function | exo-alpha-sialidase activity |
| H | 0005975 | biological_process | carbohydrate metabolic process |
| H | 0016020 | cellular_component | membrane |
| H | 0033644 | cellular_component | host cell membrane |
| H | 0046761 | biological_process | viral budding from plasma membrane |
| H | 0055036 | cellular_component | virion membrane |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | ASP151 | |
| B | ASP151 | |
| C | ASP151 | |
| D | ASP151 | |
| E | ASP151 | |
| F | ASP151 | |
| G | ASP151 | |
| H | ASP151 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | TYR406 | |
| B | TYR406 | |
| C | TYR406 | |
| D | TYR406 | |
| E | TYR406 | |
| F | TYR406 | |
| G | TYR406 | |
| H | TYR406 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071 |
| Chain | Residue | Details |
| A | ARG118 | |
| B | ARG371 | |
| C | ARG118 | |
| C | ARG152 | |
| C | GLU276 | |
| C | ARG292 | |
| C | ARG371 | |
| D | ARG118 | |
| D | ARG152 | |
| D | GLU276 | |
| D | ARG292 | |
| A | ARG152 | |
| D | ARG371 | |
| E | ARG118 | |
| E | ARG152 | |
| E | GLU276 | |
| E | ARG292 | |
| E | ARG371 | |
| F | ARG118 | |
| F | ARG152 | |
| F | GLU276 | |
| F | ARG292 | |
| A | GLU276 | |
| F | ARG371 | |
| G | ARG118 | |
| G | ARG152 | |
| G | GLU276 | |
| G | ARG292 | |
| G | ARG371 | |
| H | ARG118 | |
| H | ARG152 | |
| H | GLU276 | |
| H | ARG292 | |
| A | ARG292 | |
| H | ARG371 | |
| A | ARG371 | |
| B | ARG118 | |
| B | ARG152 | |
| B | GLU276 | |
| B | ARG292 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| 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 |
| A | ASP293 | |
| C | GLY297 | |
| C | ASP324 | |
| C | ASN347 | |
| D | ASP293 | |
| D | GLY297 | |
| D | ASP324 | |
| D | ASN347 | |
| E | ASP293 | |
| E | GLY297 | |
| E | ASP324 | |
| A | GLY297 | |
| E | ASN347 | |
| F | ASP293 | |
| F | GLY297 | |
| F | ASP324 | |
| F | ASN347 | |
| G | ASP293 | |
| G | GLY297 | |
| G | ASP324 | |
| G | ASN347 | |
| H | ASP293 | |
| A | ASP324 | |
| H | GLY297 | |
| H | ASP324 | |
| H | ASN347 | |
| A | ASN347 | |
| B | ASP293 | |
| B | GLY297 | |
| B | ASP324 | |
| B | ASN347 | |
| C | ASP293 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| 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 |
| A | ASN86 | |
| D | ASN86 | |
| D | ASN146 | |
| D | ASN200 | |
| E | ASN86 | |
| E | ASN146 | |
| E | ASN200 | |
| F | ASN86 | |
| F | ASN146 | |
| F | ASN200 | |
| G | ASN86 | |
| A | ASN146 | |
| G | ASN146 | |
| G | ASN200 | |
| H | ASN86 | |
| H | ASN146 | |
| H | ASN200 | |
| A | ASN200 | |
| B | ASN86 | |
| B | ASN146 | |
| B | ASN200 | |
| C | ASN86 | |
| C | ASN146 | |
| C | ASN200 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| A | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| A | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| A | ARG292 | electrostatic stabiliser |
| A | ARG371 | electrostatic stabiliser |
| A | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| B | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| B | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| B | ARG292 | electrostatic stabiliser |
| B | ARG371 | electrostatic stabiliser |
| B | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| C | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| C | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| C | ARG292 | electrostatic stabiliser |
| C | ARG371 | electrostatic stabiliser |
| C | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| D | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| D | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| D | ARG292 | electrostatic stabiliser |
| D | ARG371 | electrostatic stabiliser |
| D | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| E | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| E | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| E | ARG292 | electrostatic stabiliser |
| E | ARG371 | electrostatic stabiliser |
| E | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| F | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| F | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| F | ARG292 | electrostatic stabiliser |
| F | ARG371 | electrostatic stabiliser |
| F | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA7 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| G | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| G | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| G | ARG292 | electrostatic stabiliser |
| G | ARG371 | electrostatic stabiliser |
| G | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA8 |
| Number of Residues | 5 |
| Details | M-CSA 828 |
| Chain | Residue | Details |
| H | ASP151 | activator, electrostatic stabiliser, increase acidity, increase nucleophilicity, proton acceptor, proton donor |
| H | GLU277 | activator, electrostatic stabiliser, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor |
| H | ARG292 | electrostatic stabiliser |
| H | ARG371 | electrostatic stabiliser |
| H | TYR406 | electrostatic stabiliser, nucleofuge, nucleophile, proton acceptor, proton donor |
