PPIRE01075
Target Protein Information
| Protein_Name | Protein phosphatase 1A |
|---|---|
| Protein_Sequence | MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLESWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFKGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPNAPKVSPEAVKKEAELDKYLECRVEEIIKKQGEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSTSTDDMW |
| Organism_Source | Homo sapiens |
| Functional_Classification | phosphatases |
| Cellular_Localization | Cytoplasm |
| Gene_Names | PPM1A |
| UniProt_ID | P35813 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | p38(175-185 |
|---|---|
| Peptide_Sequence | TDDEMXGYVAT |
| Peptide_Length | 11 |
| Peptide_SMILES | CSCC[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)NCC(=O)NCC(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)N[C@H](C(=O)O)[C@@H](C)O)C(C)C |
| Chemical_Modification | X6=phosphothreonine |
| 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 | 1158.20 |
|---|---|
| Aliphatic_Index | 35.45455 |
| Aromaticity | 0.09091 |
| Average_Rotatable_Bonds | 3.27273 |
| Charge_at_pH_7 | -3.00020 |
| Isoelectric_Point | 3.38003 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 19 |
| Number_of_Hydrogen_Bond_Donors | 18 |
| Topological_Polar_Surface_Area | 526.91000 |
| X_logP_energy | -6.53780 |
Interaction Information
| Affinity | KD=48 uM |
|---|---|
| Affinity_Assay | fluorescence anisotropy |
| PDB_ID | None |
| Type | substrate |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | A trapped human PPM1A-phosphopeptide complex reveals structural features critical for regulation of PPM protein phosphatase activity. |
| Release_Year | 2018 |
| PMID | 29602904 |
| DOI | 10.1074/jbc.RA117.001213 |