1I3O
CRYSTAL STRUCTURE OF THE COMPLEX OF XIAP-BIR2 AND CASPASE 3
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 ZN E 1 |
| Chain | Residue |
| E | CYS200 |
| E | CYS203 |
| E | HIS220 |
| E | CYS227 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN F 2 |
| Chain | Residue |
| F | CYS200 |
| F | CYS203 |
| F | HIS220 |
| F | CYS227 |
Functional Information from PROSITE/UniProt
| site_id | PS01121 |
| Number of Residues | 15 |
| Details | CASPASE_HIS Caspase family histidine active site. HskrsSfvCvLLSHG |
| Chain | Residue | Details |
| A | HIS224-GLY238 |
| site_id | PS01282 |
| Number of Residues | 68 |
| Details | BIR_REPEAT_1 BIR repeat. EeaRlksfqn.Wpdyahltprelas.AGLyYtgigDqvqCfaCggklknWepgdrawseHrrhfPnCffV |
| Chain | Residue | Details |
| E | GLU163-VAL230 |
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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 67 |
| Details | Repeat: {"description":"BIR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 16 |
| Details | Region: {"description":"Interaction with caspase-7"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| A | THR177 | electrostatic stabiliser |
| A | SER178 | electrostatic stabiliser |
| A | HIS237 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLY238 | electrostatic stabiliser |
| A | ALA285 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | |
| Details | M-CSA 815 |
| Chain | Residue | Details |
| C | THR177 | electrostatic stabiliser |
| C | SER178 | electrostatic stabiliser |
| C | HIS237 | electrostatic stabiliser, proton acceptor, proton donor |
| C | GLY238 | electrostatic stabiliser |
| C | ALA285 | electrostatic stabiliser |
