PPIRE03040

Target Protein Information
Protein_Name Protein enabled homolog
Protein_Sequence MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAAQSKVTATQDSTNLRCIFCGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQERERERLEQLEREQVEWERERRMSNAAPSSDSSLSSAPLPEYSSCQPPSAPPPSYAKVISAPVSDATPDYAVVTALPPTSTPPTPPLRHAATRFATSLGSAFHPVLPHYATVPRPLNKNSRPSSPVNTPSSQPPAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCVSSPVPQMPPSPTAPNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPLPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAGAPASAETPLNPELGDSSASEPGLQAASQPAESPTPQGLVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSTGPPPPPPPPPPLPNQAPPPPPPPPAPPLPASGIFSGSTSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPGGGNTGSVSLASSKADAGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRNEDAEPITAKAPSTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA
Organism_Source Mus musculus
Functional_Classification E3 ubiquitin ligase adaptors
Cellular_Localization Cytoplasm
Gene_Names Enah
UniProt_ID Q03173
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name ActA peptide
Peptide_Sequence DFPPPPTDEEL
Peptide_Length 11
Peptide_SMILES CC(C)C[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](NC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)CC(=O)O)[C@@H](C)O)C(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1256.33
Aliphatic_Index 35.45455
Aromaticity 0.09091
Average_Rotatable_Bonds 2.90909
Charge_at_pH_7 -3.99757
Isoelectric_Point 3.29497
Number_of_Hydrogen_Bond_Acceptors 17
Number_of_Hydrogen_Bond_Donors 13
Topological_Polar_Surface_Area 488.59000
X_logP_energy -3.38030
Interaction Information
Affinity KD=5 uM
Affinity_Assay Bio-Layer Interferometry
PDB_ID None
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly.
Release_Year 1999
PMID 10338211
DOI 10.1016/s0092-8674(00)80757-6