PPIRE08831

Target Protein Information
Protein_Name Ribonucleoside-diphosphate reductase 1 subunit beta
Protein_Sequence MAYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL
Organism_Source Escherichia coli (strain K12)
Functional_Classification oxidoreductases
Cellular_Localization Cytoplasm
Gene_Names nrdB
UniProt_ID P69924
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name E. coli Ac-nonapeptide
Peptide_Sequence TDDLSNFQL
Peptide_Length 9
Peptide_SMILES CC(C)C[C@H](NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)[C@@H](C)O)C(=O)O
Chemical_Modification None
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Acetyl
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1052.11
Aliphatic_Index 86.66667
Aromaticity 0.11111
Average_Rotatable_Bonds 3.77778
Charge_at_pH_7 -2.00112
Isoelectric_Point 3.49188
Number_of_Hydrogen_Bond_Acceptors 16
Number_of_Hydrogen_Bond_Donors 16
Topological_Polar_Surface_Area 497.36000
X_logP_energy -5.92500
Interaction Information
Affinity IC50=400 pM
Affinity_Assay Enzyme Inhibition Kinetics
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title Specific inhibition of ribonucleotide reductases by peptides corresponding to the C-terminal of their second subunit.
Release_Year 1991
PMID 2043345
DOI 10.1139/o91-011