PPIRE17312

Target Protein Information
Protein_Name Chaperonin GroEL
Protein_Sequence MAAKDVKFGNDARVKMLRGVNVLADAVKVTLGPKGRNVVLDKSFGAPTITKDGVSVAREIELEDKFENMGAQMVKEVASKANDAAGDGTTTATVLAQAIITEGLKAVAAGMNPMDLKRGIDKAVTAAVEELKALSVPCSDSKAIAQVGTISANSDETVGKLIAEAMDKVGKEGVITVEDGTGLQDELDVVEGMQFDRGYLSPYFINKPETGAVELESPFILLADKKISNIREMLPVLEAVAKAGKPLLIIAEDVEGEALATLVVNTMRGIVKVAAVKAPGFGDRRKAMLQDIATLTGGTVISEEIGMELEKATLEDLGQAKRVVINKDTTTIIDGVGEEAAIQGRVAQIRQQIEEATSDYDREKLQERVAKLAGGVAVIKVGAATEVEMKEKKARVEDALHATRAAVEEGVVAGGGVALIRVASKLADLRGQNEDQNVGIKVALRAMEAPLRQIVLNCGEEPSVVANTVKGGDGNYGYNAATEEYGNMIDMGILDPTKVTRSALQYAASVAGLMITTECMVTDLPKNDAADLGAAGGMGGMGGMGGMM
Organism_Source Escherichia coli (strain K12)
Functional_Classification chaperonins
Cellular_Localization Cytoplasm
Gene_Names groEL
UniProt_ID P0A6F5
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name SBP
Peptide_Sequence SWMTTPWGFLHP
Peptide_Length 12
Peptide_SMILES CSCC[C@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@@H](N)CO)C(=O)N[C@H](C(=O)N[C@H](C(=O)N1CCC[C@H]1C(=O)N[C@@H](Cc1c[nH]c2ccccc12)C(=O)NCC(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)N1CCC[C@H]1C(=O)O)[C@@H](C)O)[C@@H](C)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 1459.69
Aliphatic_Index 32.50000
Aromaticity 0.25000
Average_Rotatable_Bonds 3.08333
Charge_at_pH_7 0.08889
Isoelectric_Point 7.55032
Number_of_Hydrogen_Bond_Acceptors 18
Number_of_Hydrogen_Bond_Donors 17
Topological_Polar_Surface_Area 486.79000
X_logP_energy -1.41550
Interaction Information
Affinity KD=2 mM
Affinity_Assay Fluorescence Polarization
PDB_ID None
Type Inhibitor
Structure
Reference Information
Document_Type Research Articles
Title The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity
Release_Year 1999
PMID 10619429
DOI 10.1016/s0092-8674(00)81673-6