PPIRE14391

Target Protein Information
Protein_Name mRNA interferase toxin RelE
Protein_Sequence MAYFLDFDERALKEWRKLGSTVREQLKKKLVEVLESPRIEANKLRGMPDCYKIKLRSSGYRLVYQVIDEKVVVFVISVGKRERSEVYSEAVKRIL
Organism_Source Escherichia coli (strain K12)
Functional_Classification ribonucleases
Cellular_Localization Cytoplasm
Gene_Names relE
UniProt_ID P0C077
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name RelBC
Peptide_Sequence KFEQERANAGIVLVGDVERIIAGVSLAEQLAEK
Peptide_Length 33
Peptide_SMILES CC[C@H](C)[C@H](NC(=O)CNC(=O)[C@H](C)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@@H](N)CCCCN)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C(=O)NCC(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCNC(=N)N)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](C)C(=O)NCC(=O)N[C@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)C(C)C)[C@@H](C)CC)[C@@H](C)CC)C(C)C)C(C)C)C(C)C
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 3554.06
Aliphatic_Index 121.21212
Aromaticity 0.03030
Average_Rotatable_Bonds 3.78788
Charge_at_pH_7 -1.99329
Isoelectric_Point 4.41433
Number_of_Hydrogen_Bond_Acceptors 48
Number_of_Hydrogen_Bond_Donors 52
Topological_Polar_Surface_Area 1543.66000
X_logP_energy -13.96916
Interaction Information
Affinity KD=154 nM
Affinity_Assay intrinsic tryptophan fluorescence
PDB_ID 2KC8
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site.
Release_Year 2009
PMID 19297318
DOI 10.1074/jbc.M809656200