3TRS
The crystal structure of aspergilloglutamic peptidase from Aspergillus niger
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006508 | biological_process | proteolysis |
| A | 0070007 | molecular_function | glutamic-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0070007 | molecular_function | glutamic-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0070007 | molecular_function | glutamic-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0070007 | molecular_function | glutamic-type endopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS A 201 |
| Chain | Residue |
| A | TRP7 |
| B | GLY15 |
| B | ASP16 |
| B | MET149 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS D 200 |
| Chain | Residue |
| D | HOH221 |
| D | HOH224 |
| D | HOH233 |
| D | TYR50 |
| D | HIS90 |
| D | PHE92 |
| D | SER156 |
| D | HOH184 |
