4XMI
Crystal structure of the K499G mutant of NanB sialidase from Streptococcus pneumoniae
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 | 3 |
| Details | binding site for residue DMS A 701 |
| Chain | Residue |
| A | PHE105 |
| A | ARG107 |
| A | GLU115 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 702 |
| Chain | Residue |
| A | ARG129 |
| A | GLU165 |
| A | VAL166 |
| A | SER682 |
| A | HOH1324 |
| A | HOH823 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue DMS A 703 |
| Chain | Residue |
| A | TYR160 |
| A | GLY163 |
| A | ASP217 |
| A | VAL220 |
| A | HOH1188 |
| A | HOH1276 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue PO4 A 704 |
| Chain | Residue |
| A | ARG245 |
| A | ILE246 |
| A | ARG264 |
| A | ASP270 |
| A | ILE326 |
| A | ASP327 |
| A | GLU541 |
| A | TYR653 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 705 |
| Chain | Residue |
| A | TYR250 |
| A | THR251 |
| A | GLN494 |
| A | THR657 |
| A | HOH1182 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 706 |
| Chain | Residue |
| A | GLU194 |
| A | ASP448 |
| A | LEU450 |
| A | HOH873 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue DMS A 707 |
| Chain | Residue |
| A | PHE294 |
| A | ALA295 |
| A | MET296 |
| A | LYS297 |
| A | TRP471 |
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 |
