4HQ0
Crystal Structure of mutant form of Caspase-7
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 PROSITE/UniProt
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:15314233 |
Chain | Residue | Details |
A | HIS144 | |
B | HIS144 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:16916640 |
Chain | Residue | Details |
A | CYS186 | |
B | CYS186 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by CAPN1 => ECO:0000269|PubMed:19617626 |
Chain | Residue | Details |
A | SER47 | |
B | SER47 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Involved in allosteric regulation => ECO:0000269|PubMed:15314233, ECO:0000269|PubMed:19581639 |
Chain | Residue | Details |
A | ARG187 | |
A | TYR223 | |
B | ARG187 | |
B | TYR223 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207 |
Chain | Residue | Details |
A | THR173 | |
B | THR173 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120 |
Chain | Residue | Details |
A | ARG233 | |
B | ARG233 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21555521, ECO:0000269|PubMed:27889207 |
Chain | Residue | Details |
A | SER239 | |
B | SER239 |