PPIRE12381
Target Protein Information
| Protein_Name | Chemotaxis protein CheY |
|---|---|
| Protein_Sequence | MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM |
| Organism_Source | Escherichia coli (strain K12) |
| Functional_Classification | response regulators |
| Cellular_Localization | Cytoplasm |
| Gene_Names | cheY |
| UniProt_ID | P0AE67 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | FliM peptide |
|---|---|
| Peptide_Sequence | MGDSILSQAEIDALLN |
| Peptide_Length | 16 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CO)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](NC(=O)[C@H](CO)NC(=O)[C@H](CC(=O)O)NC(=O)CNC(=O)[C@@H](N)CCSC)[C@@H](C)CC)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)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 | 1689.90 |
|---|---|
| Aliphatic_Index | 134.37500 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 3.62500 |
| Charge_at_pH_7 | -2.99935 |
| Isoelectric_Point | 3.38003 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 25 |
| Number_of_Hydrogen_Bond_Donors | 24 |
| Topological_Polar_Surface_Area | 738.36000 |
| X_logP_energy | -7.73520 |
Interaction Information
| Affinity | KD=21 uM |
|---|---|
| Affinity_Assay | Isothermal titration calorimetry |
| PDB_ID | None |
| Type | Affinity ligand |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | The structures of T87I phosphono-CheY and T87I/Y106W phosphono-CheY help to explain their binding affinities to the FliM and CheZ peptides. |
| Release_Year | 2008 |
| PMID | 18801331 |
| DOI | 10.1016/j.abb.2008.08.019 |