PPIRE08265

Target Protein Information
Protein_Name Alkaline phosphatase
Protein_Sequence MKQSTIALALLPLLFTPVTKARTPEMPVLENRAAQGDITAPGGARRLTGDQTAALRDSLSDKPAKNIILLIGDGMGDSEITAARNYAEGAGGFFKGIDALPLTGQYTHYALNKKTGKPDYVTDSAASATAWSTGVKTYNGALGVDIHEKDHPTILEMAKAAGLATGNVSTAELQDATPAALVAHVTSRKCYGPSATSEKCPGNALEKGGKGSITEQLLNARADVTLGGGAKTFAETATAGEWQGKTLREQAQARGYQLVSDAASLNSVTEANQQKPLLGLFADGNMPVRWLGPKATYHGNIDKPAVTCTPNPQRNDSVPTLAQMTDKAIELLSKNEKGFFLQVEGASIDKQDHAANPCGQIGETVDLDEAVQRALEFAKKEGNTLVIVTADHAHASQIVAPDTKAPGLTQALNTKDGAVMVMSYGNSEEDSQEHTGSQLRIAAYGPHAANVVGLTDQTDLFYTMKAALGLK
Organism_Source Escherichia coli (strain K12)
Functional_Classification phosphatases
Cellular_Localization Extracellular
Gene_Names phoA
UniProt_ID P00634
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name P2
Peptide_Sequence ADEYLIPQQ
Peptide_Length 9
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)[C@H](CC(C)C)NC(=O)[C@H](Cc1ccc(O)cc1)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](C)N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(N)=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 1076.17
Aliphatic_Index 97.77778
Aromaticity 0.11111
Average_Rotatable_Bonds 3.66667
Charge_at_pH_7 -2.00064
Isoelectric_Point 3.55007
Number_of_Hydrogen_Bond_Acceptors 15
Number_of_Hydrogen_Bond_Donors 14
Topological_Polar_Surface_Area 468.34000
X_logP_energy -3.28620
Interaction Information
Affinity KD=40.8 uM
Affinity_Assay Surface plasmon resonance
PDB_ID None
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title Development of a universal phosphorylated peptide-binding protein for simultaneous assay of kinases.
Release_Year 2009
PMID 19349157
DOI 10.1016/j.bios.2009.02.020