5L6Z
Crystal structure of D62A mutant of Thermotoga maritima TmPEP1050 aminopeptidase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008152 | biological_process | metabolic process |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008810 | molecular_function | cellulase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008152 | biological_process | metabolic process |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008810 | molecular_function | cellulase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue CIT A 401 |
| Chain | Residue |
| A | LYS93 |
| B | LYS93 |
| B | ARG94 |
| B | ASP152 |
| B | SER153 |
| B | PRO309 |
| B | HOH404 |
| A | ARG94 |
| A | ASP152 |
| A | SER153 |
| A | HOH503 |
| A | HOH505 |
| A | HOH509 |
| A | HOH517 |
| A | HOH582 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 402 |
| Chain | Residue |
| A | LEU26 |
| A | GLU30 |
| A | HOH818 |
| A | HOH826 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 403 |
| Chain | Residue |
| A | GLU63 |
| A | ILE64 |
| A | ASP168 |
| A | HOH571 |
| A | HOH778 |
