PPIRE10210

Target Protein Information
Protein_Name Chaperone protein DnaK
Protein_Sequence MGKIIGIDLGTTNSCVAIMDGTTPRVLENAEGDRTTPSIIAYTQDGETLVGQPAKRQAVTNPQNTLFAIKRLIGRRFQDEEVQRDVSIMPFKIIAADNGDAWVEVKGQKMAPPQISAEVLKKMKKTAEDYLGEPVTEAVITVPAYFNDAQRQATKDAGRIAGLEVKRIINEPTAAALAYGLDKGTGNRTIAVYDLGGGTFDISIIEIDEVDGEKTFEVLATNGDTHLGGEDFDSRLINYLVEEFKKDQGIDLRNDPLAMQRLKEAAEKAKIELSSAQQTDVNLPYITADATGPKHMNIKVTRAKLESLVEDLVNRSIEPLKVALQDAGLSVSDIDDVILVGGQTRMPMVQKKVAEFFGKEPRKDVNPDEAVAIGAAVQGGVLTGDVKDVLLLDVTPLSLGIETMGGVMTTLIAKNTTIPTKHSQVFSTAEDNQSAVTIHVLQGERKRAADNKSLGQFNLDGINPAPRGMPQIEVTFDIDADGILHVSAKDKNSGKEQKITIKASSGLNEDEIQKMVRDAEANAEADRKFEELVQTRNQGDHLLHSTRKQVEEAGDKLPADDKTAIESALTALETALKGEDKAAIEAKMQELAQVSQKLMEIAQQQHAQQQTAGADASANNAKDDDVVDAEFEEVKDKK
Organism_Source Escherichia coli O157:H7
Functional_Classification chaperone (Hsp70)
Cellular_Localization Cytoplasm
Gene_Names dnaK
UniProt_ID P0A6Z0
Protein-Protein Interaction Networks
Peptide Basic Information
Peptide_Name pyrrhocoricin(1-11)_LYZ
Peptide_Sequence VDKLYXLPRPT
Peptide_Length 11
Peptide_SMILES CC(C)C[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)NC(=O)[C@@H](N)C(C)C)C(=O)N[C@@H](Cc1ccc(O)cc1)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCNC(=N)N)C(=O)N1CCC[C@H]1C(=O)N[C@H](C(=O)O)[C@@H](C)O
Chemical_Modification Z=cyclohexylalanine
Cyclization_Method None
Linear/Cyclic Linear
N-terminal_Modification Free
C-terminal_Modification Free
Amino_Acid_Distribution
Peptide Physicochemical
Molecular_Weight 1258.48
Aliphatic_Index 97.27273
Aromaticity 0.09091
Average_Rotatable_Bonds 3.36364
Charge_at_pH_7 0.99728
Isoelectric_Point 9.29736
Number_of_Hydrogen_Bond_Acceptors 17
Number_of_Hydrogen_Bond_Donors 17
Topological_Polar_Surface_Area 502.42000
X_logP_energy -3.16563
Interaction Information
Affinity KD=0.41 uM
Affinity_Assay Fluorescence Polarization
PDB_ID None
Type Affinity ligand
Structure
Reference Information
Document_Type Research Articles
Title Structural studies on the forward and reverse binding modes of peptides to the chaperone DnaK.
Release_Year 2013
PMID 23562829
DOI 10.1016/j.jmb.2013.03.041