PPIPT00993

Target Protein Information
Protein_Name LexA repressor
Protein_Sequence MKALTARQQEVFDLIRDHISQTGMPPTRAEIAQRLGFRSPNAAEEHLKALARKGVIEIVSGASRGIRLLQEEEEGLPLVGRVAAGEPLLAQQHIEGHYQVDPSLFKPNADFLLRVSGMSMKDIGIMDGDLLAVHKTQDVRNGQVVVARIDDEVTVKRLKKQGNKVELLPENSEFKPIVVDLRQQSFTIEGLAVGVIRNGDWL
Organism_Source Escherichia coli (strain SE11)
Functional_Classification Helixurnelix transcriptional repressor
Cellular_Localization Cytoplasm
Gene_Names lexA
UniProt_ID B6I5Q8
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name L2
Peptide_Sequence SRSWDLPGEY
Peptide_Length 10
Peptide_SMILES CC(C)C[C@H](NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CO)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H](N)CO)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Cyclic
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1209.28
Aliphatic_Index 39.00000
Aromaticity 0.20000
Average_Rotatable_Bonds 3.50000
Charge_at_pH_7 -1.00065
Isoelectric_point 4.18441
Number_of_Hydrogen_Bond_Acceptors 17
Number_of_Hydrogen_Bond_Donors 19
Topological_Polar_Surface_Area 529.41000
X_logP_energy -4.79513
Interaction Information
Affinity KD=1.7 uM
Affinity_Assay Surface Plasmon Resonance
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Patent
Title STABILIZATION OF CYCLIC PEPTIDE STRUCTURES
Release_Year 2010
Patent_ID US20100129807A1