PPIRE12250
Target Protein Information
| Protein_Name | Metallothionein-3 |
|---|---|
| Protein_Sequence | MDPETCPCPSGGSCTCADSCKCEGCKCTSCKKSCCSCCPAECEKCAKDCVCKGGEAAEAEAEKCSCCQ |
| Organism_Source | Homo sapiens |
| Functional_Classification | metal-binding proteins |
| Cellular_Localization | Extracellular |
| Gene_Names | MT3 |
| UniProt_ID | P25713 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Abeta1-16(Y10A) |
|---|---|
| Peptide_Sequence | DAEFRHDSGAEVHHQK |
| Peptide_Length | 16 |
| Peptide_SMILES | CC(C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)CNC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1c[nH]cn1)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC(=O)O)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCCCN)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 1862.94 |
|---|---|
| Aliphatic_Index | 30.62500 |
| Aromaticity | 0.06250 |
| Average_Rotatable_Bonds | 3.87500 |
| Charge_at_pH_7 | -1.72514 |
| Isoelectric_Point | 6.21402 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 28 |
| Number_of_Hydrogen_Bond_Donors | 30 |
| Topological_Polar_Surface_Area | 886.30000 |
| X_logP_energy | -10.53333 |
Interaction Information
| Affinity | KD=83 uM |
|---|---|
| Affinity_Assay | Surface plasmon resonance |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Metal-dependent interactions of metallothionein-3 Beta-domain with amyloid-Beta peptide and related physiological implications. |
| Release_Year | 2019 |
| PMID | 31005822 |
| DOI | 10.1016/j.jinorgbio.2019.110693 |