Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 218 |
| site_id | PRO |
| Number of Residues | 4 |
| Details | CYS-HIS DYAD AND STABILIZING ELECTROSTATIC ENVIRONMENT (CYS 172, HIS 44, TYR 143). |
| Chain | Residue |
| A | CYS172 |
| A | HIS44 |
| A | TYR143 |
| A | HOH223 |
| site_id | RNA |
| Number of Residues | 4 |
| Details | CONSERVED SEQUENCE MOTIF KFRDI ON SURFACE OPPOSITE FROM PROTEOLYTIC ACTIVE SITE (LYS 95 TO ILE 99). |
| Chain | Residue |
| A | ARG97 |
| A | ASP98 |
| A | HOH223 |
| A | LYS95 |
| site_id | S1 |
| Number of Residues | 4 |
| Details | HIS 191 IN A POSITION TO HYDROGEN-BOND TO GLUTAMINE RESIDUE IN P1 POSITION OF PEPTIDE SUBSTRATE. |
| Chain | Residue |
| A | HIS191 |
| A | GLU132 |
| A | HOH221 |
| A | HOH226 |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | HIS44 | |
| B | ASP84 | |
| B | OCS172 | |
