4JR1
Human procaspase-7 bound to Ac-DEVD-CMK
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 | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 401 |
| Chain | Residue |
| A | LYS76 |
| A | GLY89 |
| A | THR90 |
| A | ASP91 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 401 |
| Chain | Residue |
| B | LYS76 |
| B | ASN88 |
| B | GLY89 |
| B | THR90 |
| B | ASP91 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR CHAIN C OF AC-DEVD-CMK |
| Chain | Residue |
| A | ARG87 |
| A | HIS144 |
| A | GLY145 |
| A | GLN184 |
| A | CYS186 |
| A | TYR230 |
| A | SER231 |
| A | TRP232 |
| A | ARG233 |
| A | SER234 |
| A | PRO235 |
| A | TRP240 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR CHAIN D OF AC-DEVD-CMK |
| Chain | Residue |
| B | ARG87 |
| B | HIS144 |
| B | GLY145 |
| B | GLN184 |
| B | CYS186 |
| B | TYR230 |
| B | SER231 |
| B | TRP232 |
| B | ARG233 |
| B | PRO235 |
| B | SER275 |
| B | GLN276 |
| D | HOH201 |
| D | HOH202 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Region: {"description":"Loop L1","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Region: {"description":"Loop L3","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"11701129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16916640","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Involved in allosteric regulation","evidences":[{"source":"PubMed","id":"15314233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19581639","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Microbial infection) ADP-riboxanated arginine","evidences":[{"source":"PubMed","id":"35338844","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35446120","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21555521","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27889207","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 14 |
| Details | Region: {"description":"Loop L4","evidences":[{"source":"PubMed","id":"23897474","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
