Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE DTD B 505 |
| Chain | Residue |
| A | TYR334 |
| A | THR337 |
| B | GLU396 |
| B | PHE399 |
| B | LEU401 |
| B | THR469 |
| B | HOH657 |
| B | HOH681 |
| B | HOH690 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DTD A 506 |
| Chain | Residue |
| A | LYS231 |
| A | PRO232 |
| A | HIS278 |
| A | GLU290 |
| A | GLU294 |
| A | HOH714 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR CHAIN C OF ACETYL-ILE-GLU-THR-ASP-ALDEHYDE |
| Chain | Residue |
| A | ARG260 |
| A | HIS317 |
| A | GLY318 |
| A | GLN358 |
| A | CYS360 |
| A | HOH694 |
| B | SER411 |
| B | TYR412 |
| B | ARG413 |
| B | PRO415 |
| B | TRP420 |
| B | HOH665 |
| C | HOH632 |
| C | HOH675 |
| C | HOH677 |
| C | HOH759 |
| C | HOH797 |
| C | HOH878 |
| C | HOH890 |
| C | HOH909 |
| C | HOH914 |
Functional Information from PROSITE/UniProt
| site_id | PS01121 |
| Number of Residues | 15 |
| Details | CASPASE_HIS Caspase family histidine active site. HsnmdCfiCcILSHG |
| Chain | Residue | Details |
| A | HIS304-GLY318 | |
| site_id | PS01122 |
| Number of Residues | 12 |
| Details | CASPASE_CYS Caspase family cysteine active site. KPKVFFIQACQG |
| Chain | Residue | Details |
| A | LYS351-GLY362 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"10508785","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"O89110","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10508785 |
| Chain | Residue | Details |
| A | GLY350 | |
| A | HIS317 | |
| A | CYS360 | |
| A | ARG258 | |
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| A | ARG258 | electrostatic stabiliser |
| A | HIS317 | proton acceptor, proton donor |
| A | GLY318 | electrostatic stabiliser |
| A | CYS360 | nucleofuge, nucleophile, proton acceptor, proton donor |
