7WR6
Crystal structure of ADP-riboxanated caspase-4 in complex with Af1521
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 | 0016787 | molecular_function | hydrolase activity |
| B | 0140291 | biological_process | peptidyl-glutamate ADP-deribosylation |
| B | 0140293 | molecular_function | ADP-ribosylglutamate hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01121 |
| Number of Residues | 15 |
| Details | CASPASE_HIS Caspase family histidine active site. HkssdStfLvLMSHG |
| Chain | Residue | Details |
| A | HIS197-GLY211 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P29466","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"22246630","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23661706","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25119034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37993712","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37993714","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"7743998","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 15 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15902274","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
