6JTL
Crystal structure of NagZ from Neisseria gonorrhoeae in complex with zinc ion
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 | 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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
| A | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
| B | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| B | 0004563 | molecular_function | beta-N-acetylhexosaminidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| 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 | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
| B | 0102148 | molecular_function | N-acetyl-beta-D-galactosaminidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | HIS175 |
| A | HOH573 |
| A | HOH633 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue ZN A 402 |
| Chain | Residue |
| A | HIS179 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN B 401 |
| Chain | Residue |
| B | HIS175 |
| B | HOH561 |
| B | HOH566 |
| B | HOH568 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue ZN B 402 |
| Chain | Residue |
| B | HOH531 |
| B | HIS179 |
Functional Information from PROSITE/UniProt
| site_id | PS00775 |
| Number of Residues | 18 |
| Details | GLYCOSYL_HYDROL_F3 Glycosyl hydrolases family 3 active site. ILRrDigfkGVIFSDdlT |
| Chain | Residue | Details |
| A | ILE244-THR261 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000255|HAMAP-Rule:MF_00364 |
| Chain | Residue | Details |
| A | HIS187 | |
| B | HIS187 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00364 |
| Chain | Residue | Details |
| A | ASP258 | |
| B | ASP258 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00364 |
| Chain | Residue | Details |
| A | ASP69 | |
| A | ARG77 | |
| A | ARG144 | |
| A | LYS174 | |
| B | ASP69 | |
| B | ARG77 | |
| B | ARG144 | |
| B | LYS174 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_00364 |
| Chain | Residue | Details |
| A | ASP185 | |
| B | ASP185 |
