3LZK
The crystal structure of a probably aromatic amino acid degradation proteiN from Sinorhizobium meliloti 1021
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 339 |
| Chain | Residue |
| A | ASP83 |
| A | GLU139 |
| A | GLU141 |
| A | ASP170 |
| A | HOH427 |
| A | HOH429 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 339 |
| Chain | Residue |
| B | ASP170 |
| B | LYS191 |
| B | HOH388 |
| B | HOH400 |
| B | ASP83 |
| B | GLU139 |
| B | GLU141 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA C 339 |
| Chain | Residue |
| C | ASP83 |
| C | GLU139 |
| C | GLU141 |
| C | ASP170 |
| C | HOH354 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 339 |
| Chain | Residue |
| D | ASP83 |
| D | GLU139 |
| D | GLU141 |
| D | ASP170 |
| D | HOH426 |
