PPIRE01076

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 c(MpSIpYVA)
Peptide_Sequence MXIXVA
Peptide_Length 6
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@@H](N)CCSC)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](C)C(=O)O)C(C)C
Chemical_Modification X2=phosphoserine; X4=phosphotyrosine
Cyclization_Method Main chain-main chain cyclization; M1<->A6; amide bond
Linear/Cyclic Cyclic
N-terminal_Modification Free
C-terminal_Modification None
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 546.68
Aliphatic_Index 130.00000
Aromaticity 0.00000
Average_Rotatable_Bonds 2.83333
Charge_at_pH_7 -0.00202
Isoelectric_Point 6.10000
Number_of_Hydrogen_Bond_Acceptors 8
Number_of_Hydrogen_Bond_Donors 7
Topological_Polar_Surface_Area 208.82000
X_logP_energy -1.43980
Interaction Information
Affinity KD=8.9 uM
Affinity_Assay Isothermal titration calorimetry
PDB_ID 6B67
Type Inhibitor
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