1V0Z
Structure of Neuraminidase from English duck subtype N6
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 | 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 | 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 | 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 | 0055036 | cellular_component | virion membrane |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ASP157 | |
B | ASP157 | |
C | ASP157 | |
D | ASP157 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | TYR412 | |
B | TYR412 | |
C | TYR412 | |
D | TYR412 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ARG124 | |
B | ARG378 | |
C | ARG124 | |
C | ARG158 | |
C | GLU283 | |
C | ARG299 | |
C | ARG378 | |
D | ARG124 | |
D | ARG158 | |
D | GLU283 | |
D | ARG299 | |
A | ARG158 | |
D | ARG378 | |
A | GLU283 | |
A | ARG299 | |
A | ARG378 | |
B | ARG124 | |
B | ARG158 | |
B | GLU283 | |
B | ARG299 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ASP300 | |
D | ASP300 | |
D | GLY304 | |
D | ASP331 | |
A | GLY304 | |
A | ASP331 | |
B | ASP300 | |
B | GLY304 | |
B | ASP331 | |
C | ASP300 | |
C | GLY304 | |
C | ASP331 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | PRO354 | |
B | PRO354 | |
C | PRO354 | |
D | PRO354 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|Ref.7 |
Chain | Residue | Details |
A | ASN92 | |
A | ASN207 | |
B | ASN92 | |
B | ASN207 | |
C | ASN92 | |
C | ASN207 | |
D | ASN92 | |
D | ASN207 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|Ref.7, ECO:0000269|Ref.8 |
Chain | Residue | Details |
A | ASN152 | |
B | ASN152 | |
C | ASN152 | |
D | ASN152 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine; by host => ECO:0000255|HAMAP-Rule:MF_04071 |
Chain | Residue | Details |
A | ASN408 | |
B | ASN408 | |
C | ASN408 | |
D | ASN408 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
A | ASP157 | |
A | GLU284 |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
B | ASP157 | |
B | GLU284 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
C | ASP157 | |
C | GLU284 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a4g |
Chain | Residue | Details |
D | ASP157 | |
D | GLU284 |