5G1M
Crystal structure of NagZ from Pseudomonas aeruginosa
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 | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 1333 |
| Chain | Residue |
| A | ALA154 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT B 1333 |
| Chain | Residue |
| B | GLN106 |
| B | LEU110 |
| B | ASP111 |
| B | GLY304 |
| B | GLY306 |
| B | HOH2145 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT A 1334 |
| Chain | Residue |
| A | GLU45 |
| A | HOH2076 |
| A | HIS39 |
| A | GLN42 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG A 1335 |
| Chain | Residue |
| A | ALA52 |
| A | ILE53 |
| A | PRO55 |
| A | HOH2083 |
| A | HOH2322 |
| A | HOH2323 |
| B | ALA52 |
| B | ILE53 |
| B | PRO55 |
| B | HOH2094 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PEG B 1335 |
| Chain | Residue |
| B | ARG301 |
| B | HOH2286 |
Functional Information from PROSITE/UniProt
| site_id | PS00775 |
| Number of Residues | 18 |
| Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRgElkfdGVIFSDdlS |
| Chain | Residue | Details |
| A | ILE230-SER247 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]} |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_00364","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
