6BGQ
Caspase-3 Mutant - S150D
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 | 4 |
| Details | binding site for residue CL A 301 |
| Chain | Residue |
| A | LYS53 |
| A | GLY66 |
| A | THR67 |
| A | ASP68 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue AZI A 302 |
| Chain | Residue |
| A | ARG79 |
| A | ASN80 |
| A | LYS82 |
| A | HOH415 |
| D | PHE252 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue AZI A 303 |
| Chain | Residue |
| A | THR92 |
| A | GLU94 |
| A | GLU95 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue AZI A 304 |
| Chain | Residue |
| A | LYS137 |
| A | THR140 |
| A | ASN141 |
| A | ARG144 |
| B | GLU190 |
| B | PHE193 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue AZI B 301 |
| Chain | Residue |
| B | ARG241 |
| B | HOH405 |
| C | ASN35 |
| D | THR270 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue AZI B 302 |
| Chain | Residue |
| B | MET222 |
| B | GLN225 |
| B | TYR226 |
| B | ARG238 |
| B | HOH445 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue CL C 201 |
| Chain | Residue |
| C | LYS53 |
| C | GLY66 |
| C | THR67 |
| C | ASP68 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue AZI C 202 |
| Chain | Residue |
| B | PHE252 |
| C | ARG79 |
| C | ASN80 |
| C | LYS82 |
| C | HOH437 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue AZI C 203 |
| Chain | Residue |
| C | LYS137 |
| C | THR140 |
| C | ASN141 |
| C | ARG144 |
| D | GLU190 |
| D | HOH404 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue AZI C 204 |
| Chain | Residue |
| C | ILE126 |
| C | THR166 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue AZI C 205 |
| Chain | Residue |
| C | THR92 |
| C | GLU94 |
| C | ASN131 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue NA D 301 |
| Chain | Residue |
| C | THR152 |
| C | GLY153 |
| C | LYS156 |
| D | ILE187 |
| D | ALA191 |
| D | ASP192 |
| D | HOH427 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue AZI D 302 |
| Chain | Residue |
| A | ASN35 |
| B | THR270 |
| D | ARG238 |
| D | ARG241 |
| D | HOH407 |
| site_id | AD5 |
| Number of Residues | 17 |
| Details | binding site for Ac-Asp-Glu-Val-Asp-CMK chain K |
| Chain | Residue |
| A | SER58 |
| A | ARG64 |
| A | HIS121 |
| A | GLY122 |
| A | GLN161 |
| A | CYS163 |
| B | TYR204 |
| B | SER205 |
| B | TRP206 |
| B | ARG207 |
| B | ASN208 |
| B | SER209 |
| B | TRP214 |
| B | SER249 |
| B | PHE250 |
| B | HOH439 |
| K | HOH101 |
| site_id | AD6 |
| Number of Residues | 23 |
| Details | binding site for Ac-Asp-Glu-Val-Asp-CMK chain L |
| Chain | Residue |
| C | SER58 |
| C | ARG64 |
| C | HIS121 |
| C | GLY122 |
| C | GLN161 |
| C | CYS163 |
| C | HOH404 |
| C | HOH465 |
| D | TYR204 |
| D | SER205 |
| D | TRP206 |
| D | ARG207 |
| D | ASN208 |
| D | SER209 |
| D | TRP214 |
| D | SER249 |
| D | PHE250 |
| D | HOH410 |
| L | HOH101 |
| L | HOH102 |
| L | HOH103 |
| L | HOH104 |
| L | HOH105 |
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 |
| C | THR62 | electrostatic stabiliser |
| C | SER63 | electrostatic stabiliser |
| C | HIS121 | electrostatic stabiliser, proton acceptor, proton donor |
| C | GLY122 | electrostatic stabiliser |
| C | CYS163 | electrostatic stabiliser |
