6IQQ
Crystal structure of Prc with S452I and L252Y mutations in complex with NlpI
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000270 | biological_process | peptidoglycan metabolic process |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0051301 | biological_process | cell division |
| B | 0000270 | biological_process | peptidoglycan metabolic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0030674 | molecular_function | protein-macromolecule adaptor activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0051301 | biological_process | cell division |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue CA C 701 |
| Chain | Residue |
| C | GLY408 |
| C | ILE411 |
| C | PRO412 |
| C | ASP431 |
| C | ASP433 |
| C | GLN435 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA D 701 |
| Chain | Residue |
| D | ASP431 |
| D | ASP433 |
| D | GLN435 |
| D | GLY408 |
| D | ILE411 |
| D | PRO412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| C | ILE452 | |
| C | LYS477 | |
| D | ILE452 | |
| D | LYS477 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system => ECO:0000305 |
| Chain | Residue | Details |
| C | ASP463 | |
| D | ASP463 |
