4HZM
Crystal structure of Salmonella typhimurium family 3 glycoside hydrolase (NagZ) bound to N-[(3S,4R,5R,6R)-4,5-dihydroxy-6-(hydroxymethyl)piperidin-3-yl]butanamide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0009254 | biological_process | peptidoglycan turnover |
| A | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0009254 | biological_process | peptidoglycan turnover |
| B | 0016231 | molecular_function | beta-N-acetylglucosaminidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1BW A 400 |
| Chain | Residue |
| A | ILE30 |
| A | HOH616 |
| A | HOH719 |
| A | HOH898 |
| A | ASP62 |
| A | ARG133 |
| A | LYS163 |
| A | HIS164 |
| A | HIS168 |
| A | MET210 |
| A | ASP249 |
| A | HOH548 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE 1BW B 401 |
| Chain | Residue |
| B | ILE30 |
| B | ASP62 |
| B | ARG133 |
| B | LYS163 |
| B | HIS164 |
| B | HIS168 |
| B | MET210 |
| B | ASP249 |
| B | HOH565 |
| B | HOH627 |
| B | HOH788 |
| B | HOH954 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE MES B 402 |
| Chain | Residue |
| A | ARG311 |
| A | ARG312 |
| A | ASP316 |
| A | HOH771 |
| A | HOH790 |
| B | SER310 |
| B | ARG312 |
| B | HOH529 |
| B | HOH591 |
| B | HOH700 |
Functional Information from PROSITE/UniProt
| site_id | PS00775 |
| Number of Residues | 18 |
| Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. VLRqElgfdGVIFSDdlS |
| Chain | Residue | Details |
| A | VAL234-SER251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23177201","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
