2JKB
Crystal structure of Streptococcus pneumoniae NanB in complex with 2, 7-anhydro-Neu5Ac
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 | 17 |
| Details | BINDING SITE FOR RESIDUE SKD A1698 |
| Chain | Residue |
| A | ARG245 |
| A | GLU541 |
| A | ARG557 |
| A | ARG619 |
| A | TYR653 |
| A | TRP674 |
| A | HOH2457 |
| A | HOH3012 |
| A | HOH3013 |
| A | ILE246 |
| A | ARG264 |
| A | ASP270 |
| A | ILE326 |
| A | ASP327 |
| A | ASP344 |
| A | ASN352 |
| A | THR539 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A1699 |
| Chain | Residue |
| A | LEU84 |
| A | SER103 |
| A | GLU115 |
| A | TYR199 |
| A | LYS335 |
| A | HOH3014 |
| A | HOH3015 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1700 |
| Chain | Residue |
| A | TYR458 |
| A | ILE459 |
| A | LEU477 |
| A | PRO478 |
| A | PHE480 |
| A | HOH3016 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A1701 |
| Chain | Residue |
| A | VAL385 |
| A | ILE404 |
| A | ASN405 |
| A | ASP406 |
| A | TYR408 |
| A | LYS475 |
| A | HOH2629 |
| A | HOH3017 |
| A | HOH3018 |
| A | HOH3019 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1702 |
| Chain | Residue |
| A | THR251 |
| A | GLN494 |
| A | ILE596 |
| A | THR657 |
| A | HOH2956 |
| A | HOH3020 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A1703 |
| Chain | Residue |
| A | SER617 |
| A | LYS620 |
| A | SER648 |
| A | HOH2911 |
| A | HOH3021 |
| A | HOH3022 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A1704 |
| Chain | Residue |
| A | ARG256 |
| A | ASN466 |
| A | ARG467 |
| A | GLU469 |
| A | SER617 |
| A | HOH2444 |
| A | HOH3023 |
| A | HOH3024 |
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 |
