4DCP
Crystal Structure of caspase 3, L168F mutant
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 |
| D | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008234 | molecular_function | cysteine-type peptidase activity |
| E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR CHAIN C OF CASPASE INHIBITOR AC-DEVD-CHO |
| Chain | Residue |
| A | ARG64 |
| B | ASN208 |
| B | SER209 |
| B | TRP214 |
| B | SER249 |
| B | PHE250 |
| B | HOH2018 |
| C | HOH601 |
| C | HOH602 |
| C | HOH603 |
| C | HOH605 |
| A | HIS121 |
| C | HOH606 |
| A | GLY122 |
| A | GLN161 |
| A | CYS163 |
| A | HOH241 |
| B | SER205 |
| B | TRP206 |
| B | ARG207 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR CHAIN F OF CASPASE INHIBITOR AC-DEVD-CHO |
| Chain | Residue |
| D | ARG1064 |
| D | HIS1121 |
| D | GLY1122 |
| D | GLN1161 |
| D | CYS1163 |
| E | TYR1204 |
| E | SER1205 |
| E | TRP1206 |
| E | ARG1207 |
| E | ASN1208 |
| E | SER1209 |
| E | TRP1214 |
| E | SER1249 |
| E | PHE1250 |
| E | HOH1322 |
| F | HOH1601 |
| F | HOH1603 |
| F | HOH1604 |
| F | HOH1605 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"P29466","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-nitrosocysteine; in inhibited form","evidences":[{"source":"PubMed","id":"10213689","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| 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"},{"source":"PubMed","id":"36423631","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| A | THR62 | electrostatic stabiliser |
| A | SER63 | electrostatic stabiliser |
| A | HIS121 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLY122 | electrostatic stabiliser |
| A | CYS163 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| D | THR1062 | electrostatic stabiliser |
| D | SER1063 | electrostatic stabiliser |
| D | HIS1121 | electrostatic stabiliser, proton acceptor, proton donor |
| D | GLY1122 | electrostatic stabiliser |
| D | CYS1163 | electrostatic stabiliser |
