PPIRE05860
Target Protein Information
| Protein_Name | Caspase-2 |
|---|---|
| Protein_Sequence | MAAPSAGSWSTFQHKELMAADRGRRILGVCGMHPHHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKVGSFSQNVELLNLLPKRGPQAFDAFCEALRETKQGHLEDMLLTTLSGLQHVLPPLSCDYDLSLPFPVCESCPLYKKLRLSTDTVEHSLDNKDGPVCLQVKPCTPEFYQTHFQLAYRLQSRPRGLALVLSNVHFTGEKELEFRSGGDVDHSTLVTLFKLLGYDVHVLCDQTAQEMQEKLQNFAQLPAHRVTDSCIVALLSHGVEGAIYGVDGKLLQLQEVFQLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHAGSPGCEESDAGKEKLPKMRLPTRSDMICGYACLKGTAAMRNTKRGSWYIEALAQVFSERACDMHVADMLVKVNALIKDREGYAPGTEFHRCKEMSEYCSTLCRHLYLFPGHPPT |
| Organism_Source | Homo sapiens |
| Functional_Classification | cysteine protease |
| Cellular_Localization | Cytoplasm |
| Gene_Names | CASP2 |
| UniProt_ID | P42575 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | VDVAD-CHO |
|---|---|
| Peptide_Sequence | VDVAD |
| Peptide_Length | 5 |
| Peptide_SMILES | CC(C)[C@H](N)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@@H](CC(=O)O)C(=O)O)C(C)C |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Acetyl |
| C-terminal_Modification | aldehyde |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 517.54 |
|---|---|
| Aliphatic_Index | 136.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 3.00000 |
| Charge_at_pH_7 | -2.00112 |
| Isoelectric_Point | 3.49188 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 8 |
| Number_of_Hydrogen_Bond_Donors | 8 |
| Topological_Polar_Surface_Area | 254.32000 |
| X_logP_energy | -2.38120 |
Interaction Information
| Affinity | IC50=25 nM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | 3R6G |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Structural and enzymatic insights into caspase-2 protein substrate recognition and catalysis. |
| Release_Year | 2011 |
| PMID | 21828056 |
| DOI | 10.1074/jbc.M111.247627 |