6PX9
Crystal structure of procaspase-8 in complex with covalent small molecule inhibitor 63-R
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 |
| E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008234 | molecular_function | cysteine-type peptidase activity |
| F | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008234 | molecular_function | cysteine-type peptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide 63R B 600 and CYS B 360 |
| Chain | Residue |
| B | ARG260 |
| B | ALA359 |
| B | GLN361 |
| B | VAL406 |
| B | TRP420 |
| E | ASP259 |
| E | ASN261 |
| B | ASN261 |
| B | GLY262 |
| B | LEU265 |
| B | ASP266 |
| B | SER316 |
| B | HIS317 |
| B | GLY318 |
| B | GLN358 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:10508785 |
| Chain | Residue | Details |
| A | ARG258 | |
| E | LEU301 | |
| F | ARG258 | |
| F | LEU301 | |
| A | LEU301 | |
| B | ARG258 | |
| B | LEU301 | |
| C | ARG258 | |
| C | LEU301 | |
| D | ARG258 | |
| D | LEU301 | |
| E | ARG258 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | SITE: Cleavage; by CASP6 => ECO:0000269|PubMed:22858542 |
| Chain | Residue | Details |
| A | LEU315 | |
| B | LEU315 | |
| C | LEU315 | |
| D | LEU315 | |
| E | LEU315 | |
| F | LEU315 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | SITE: Cleavage; by autocatalytic cleavage => ECO:0000269|PubMed:8962078, ECO:0000269|PubMed:9184224 |
| Chain | Residue | Details |
| A | GLY325 | |
| B | GLY325 | |
| C | GLY325 | |
| D | GLY325 | |
| E | GLY325 | |
| F | GLY325 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | GLU275 | |
| B | GLU275 | |
| C | GLU275 | |
| D | GLU275 | |
| E | GLU275 | |
| F | GLU275 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:16619028, ECO:0000269|PubMed:27109099 |
| Chain | Residue | Details |
| A | GLY321 | |
| B | GLY321 | |
| C | GLY321 | |
| D | GLY321 | |
| E | GLY321 | |
| F | GLY321 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine; by CDK1 => ECO:0000269|PubMed:20937773 |
| Chain | Residue | Details |
| A | GLY328 | |
| B | GLY328 | |
| C | GLY328 | |
| D | GLY328 | |
| E | GLY328 | |
| F | GLY328 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: (Microbial infection) ADP-riboxanated arginine => ECO:0000269|PubMed:35338844, ECO:0000269|PubMed:35446120 |
| Chain | Residue | Details |
| A | VAL354 | |
| B | VAL354 | |
| C | VAL354 | |
| D | VAL354 | |
| E | VAL354 | |
| F | VAL354 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| A | ARG258 | proton acceptor, proton donor |
| A | ASP259 | electrostatic stabiliser |
| A | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| B | ARG258 | proton acceptor, proton donor |
| B | ASP259 | electrostatic stabiliser |
| B | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| C | ARG258 | proton acceptor, proton donor |
| C | ASP259 | electrostatic stabiliser |
| C | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| D | ARG258 | proton acceptor, proton donor |
| D | ASP259 | electrostatic stabiliser |
| D | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA5 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| E | ARG258 | proton acceptor, proton donor |
| E | ASP259 | electrostatic stabiliser |
| E | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
| site_id | MCSA6 |
| Number of Residues | 3 |
| Details | M-CSA 818 |
| Chain | Residue | Details |
| F | ARG258 | proton acceptor, proton donor |
| F | ASP259 | electrostatic stabiliser |
| F | LEU301 | nucleofuge, nucleophile, proton acceptor, proton donor |
