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 |
| C | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008234 | molecular_function | cysteine-type peptidase activity |
| D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MLT A 668 |
| Chain | Residue |
| A | TRP354 |
| A | ARG355 |
Functional Information from PROSITE/UniProt
| site_id | PS01121 |
| Number of Residues | 15 |
| Details | CASPASE_HIS Caspase family histidine active site. HgaldCcvVvILSHG |
| Chain | Residue | Details |
| A | HIS224-GLY238 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"15657060","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| 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 | Annotated By Reference To The Literature 1nw9 |
| Chain | Residue | Details |
| A | SER287 | |
| A | GLY238 | |
| A | HIS237 | |
| A | ARG178 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nw9 |
| Chain | Residue | Details |
| B | SER287 | |
| B | GLY238 | |
| B | HIS237 | |
| B | ARG178 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nw9 |
| Chain | Residue | Details |
| C | SER287 | |
| C | GLY238 | |
| C | HIS237 | |
| C | ARG178 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nw9 |
| Chain | Residue | Details |
| D | SER287 | |
| D | GLY238 | |
| D | HIS237 | |
| D | ARG178 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 816 |
| Chain | Residue | Details |
| A | ARG178 | electrostatic stabiliser |
| A | HIS237 | proton acceptor, proton donor |
| A | GLY238 | electrostatic stabiliser |
| A | SER287 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 816 |
| Chain | Residue | Details |
| B | ARG178 | electrostatic stabiliser |
| B | HIS237 | proton acceptor, proton donor |
| B | GLY238 | electrostatic stabiliser |
| B | SER287 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 816 |
| Chain | Residue | Details |
| C | ARG178 | electrostatic stabiliser |
| C | HIS237 | proton acceptor, proton donor |
| C | GLY238 | electrostatic stabiliser |
| C | SER287 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 816 |
| Chain | Residue | Details |
| D | ARG178 | electrostatic stabiliser |
| D | HIS237 | proton acceptor, proton donor |
| D | GLY238 | electrostatic stabiliser |
| D | SER287 | nucleofuge, nucleophile, proton acceptor, proton donor |
