4XJW
Crystal structure of the NanB sialidase from streptococcus pneumoniae in complex with Optactin at pH 7.4 in PBS with DMSO as the cryoprotectant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004308 | molecular_function | exo-alpha-sialidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0006689 | biological_process | ganglioside catabolic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0009313 | biological_process | oligosaccharide catabolic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
| A | 0052794 | molecular_function | exo-alpha-(2->3)-sialidase activity |
| A | 0052795 | molecular_function | exo-alpha-(2->6)-sialidase activity |
| A | 0052796 | molecular_function | exo-alpha-(2->8)-sialidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue OPX A 701 |
| Chain | Residue |
| A | TYR250 |
| A | HOH1035 |
| A | HOH929 |
| A | HOH882 |
| A | HOH1010 |
| A | THR251 |
| A | GLN494 |
| A | LYS499 |
| A | ILE596 |
| A | THR657 |
| A | GLU658 |
| A | LEU659 |
| A | HOH1120 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue DMS A 702 |
| Chain | Residue |
| A | ARG245 |
| A | ILE246 |
| A | ARG264 |
| A | ASP270 |
| A | ILE326 |
| A | ASP327 |
| A | TYR653 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue PO4 A 703 |
| Chain | Residue |
| A | ASN99 |
| A | TYR101 |
| A | ARG117 |
| A | ARG193 |
| A | TYR199 |
| A | LYS335 |
| A | ASN502 |
| A | HOH805 |
| A | HOH838 |
| A | HOH870 |
| A | HOH898 |
| A | HOH925 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 704 |
| Chain | Residue |
| A | TYR160 |
| A | GLY163 |
| A | ASP217 |
| A | VAL220 |
| A | HOH880 |
| A | HOH1233 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 705 |
| Chain | Residue |
| A | ASN162 |
| A | HOH844 |
| A | HOH818 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 706 |
| Chain | Residue |
| A | SER238 |
| A | PRO292 |
| A | ILE293 |
| A | PHE294 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | ASP270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| A | GLU541 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: Nucleophile => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR653 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG245 | |
| A | ARG557 | |
| A | ARG619 |
