3IJ6
CRYSTAL STRUCTURE OF AN UNCHARACTERIZED METAL-DEPENDENT HYDROLASE FROM Lactobacillus acidophilus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019748 | biological_process | secondary metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016831 | molecular_function | carboxy-lyase activity |
| B | 0019748 | biological_process | secondary metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016831 | molecular_function | carboxy-lyase activity |
| C | 0019748 | biological_process | secondary metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016831 | molecular_function | carboxy-lyase activity |
| D | 0019748 | biological_process | secondary metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 312 |
| Chain | Residue |
| A | HIS10 |
| A | HIS160 |
| A | HIS204 |
| A | ASP262 |
| A | HOH357 |
| A | HOH358 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 313 |
| Chain | Residue |
| A | GLU304 |
| A | ILE118 |
| A | ASP121 |
| A | LEU124 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 312 |
| Chain | Residue |
| B | HIS10 |
| B | HIS160 |
| B | HIS204 |
| B | ASP262 |
| B | HOH394 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA B 313 |
| Chain | Residue |
| B | ILE118 |
| B | ASP121 |
| B | LEU124 |
| B | HOH354 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 312 |
| Chain | Residue |
| C | HIS10 |
| C | HIS160 |
| C | HIS204 |
| C | ASP262 |
| C | HOH329 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 313 |
| Chain | Residue |
| C | ILE118 |
| C | ASP121 |
| C | GLU122 |
| C | LEU124 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 312 |
| Chain | Residue |
| D | HIS10 |
| D | HIS160 |
| D | HIS204 |
| D | ASP262 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 313 |
| Chain | Residue |
| D | ILE118 |
| D | ASP121 |
| D | LEU124 |
| D | HOH394 |
