PPIRE14790
Target Protein Information
| Protein_Name | Actin, alpha skeletal muscle |
|---|---|
| Protein_Sequence | MCDEDETTALVCDNGSGLVKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVMSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWITKQEYDEAGPSIVHRKCF |
| Organism_Source | Oryctolagus cuniculus |
| Functional_Classification | actins |
| Cellular_Localization | Cytoplasm |
| Gene_Names | ACTA1 |
| UniProt_ID | P68135 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | CH3 |
|---|---|
| Peptide_Sequence | VAAPAPALKDLPKVAENLKSQLEGFDSKSLKNASTQEKIILPTAEDVAAEKTQQSIFES |
| Peptide_Length | 59 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CO)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)CNC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@@H](NC(=O)[C@H](CCCCN)NC(=O)[C@@H]1CCCN1C(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)NC(=O)[C@@H]1CCCN1C(=O)[C@H](C)NC(=O)[C@H](C)NC(=O)[C@@H](N)C(C)C)C(C)C)[C@@H](C)O)[C@@H](C)CC)[C@@H](C)CC)[C@@H](C)O)C(C)C)[C@@H](C)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CO)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 | 6297.12 |
|---|---|
| Aliphatic_Index | 89.49153 |
| Aromaticity | 0.03390 |
| Average_Rotatable_Bonds | 3.64407 |
| Charge_at_pH_7 | -1.99209 |
| Isoelectric_Point | 4.60859 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 91 |
| Number_of_Hydrogen_Bond_Donors | 87 |
| Topological_Polar_Surface_Area | 2674.41000 |
| X_logP_energy | -29.35480 |
Interaction Information
| Affinity | KD=0.01 mM |
|---|---|
| Affinity_Assay | fluorescence spectroscopy |
| PDB_ID | None |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | How a single residue in individual Beta-thymosin/WH2 domains controls their functions in actin assembly. |
| Release_Year | 2012 |
| PMID | 22193718 |
| DOI | 10.1038/emboj.2011.461 |