4XE9
Crystal structure of the NanB sialidase from Streptococcus pneumoniae in complex with Optactin
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 | 0009313 | biological_process | oligosaccharide catabolic process |
A | 0016020 | cellular_component | membrane |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
A | 0052794 | molecular_function | obsolete exo-alpha-(2->3)-sialidase activity |
A | 0052795 | molecular_function | obsolete exo-alpha-(2->6)-sialidase activity |
A | 0052796 | molecular_function | obsolete exo-alpha-(2->8)-sialidase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue OPX A 701 |
Chain | Residue |
A | TYR250 |
A | HOH1033 |
A | HOH1198 |
A | HOH1058 |
A | THR251 |
A | GLN494 |
A | LYS499 |
A | THR657 |
A | GLU658 |
A | HOH1088 |
A | HOH962 |
A | HOH969 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue DMS A 702 |
Chain | Residue |
A | PHE105 |
A | ARG107 |
A | GLU115 |
A | TYR199 |
A | HOH971 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue DMS A 703 |
Chain | Residue |
A | ARG129 |
A | VAL166 |
A | ARG310 |
A | HIS680 |
A | SER682 |
A | HOH884 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue DMS A 704 |
Chain | Residue |
A | GLY163 |
A | ASP217 |
A | VAL220 |
A | HOH1409 |
site_id | AC5 |
Number of Residues | 5 |
Details | binding site for residue DMS A 705 |
Chain | Residue |
A | HIS269 |
A | ASN316 |
A | GLN318 |
A | ARG676 |
A | HOH1199 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue DMS A 706 |
Chain | Residue |
A | VAL385 |
A | GLY389 |
A | ILE404 |
A | ASN405 |
A | ASP406 |
A | TYR408 |
A | LYS475 |
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 |