PPIRE12925
Target Protein Information
| Protein_Name | Vascular endothelial growth factor A, long form |
|---|---|
| Protein_Sequence | MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQEKKSVRGKGKGQKRKRKKSRYKSWSVPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR |
| Organism_Source | Homo sapiens |
| Functional_Classification | growth factors |
| Cellular_Localization | Extracellular |
| Gene_Names | VEGFA |
| UniProt_ID | P15692 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | v106 |
|---|---|
| Peptide_Sequence | GERWCFDGPRAWVCGWEI |
| Peptide_Length | 18 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)CNC(=O)[C@H](CS)NC(=O)[C@@H](NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](C)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@H](CC(=O)O)NC(=O)[C@H](Cc1ccccc1)NC(=O)[C@H](CS)NC(=O)[C@H](Cc1c[nH]c2ccccc12)NC(=O)[C@H](CCCNC(=N)N)NC(=O)[C@H](CCC(=O)O)NC(=O)CN)C(C)C)C(=O)O |
| Chemical_Modification | None |
| Cyclization_Method | Side chain-side chain cyclization; C5<->C14; disulfide bond |
| Linear/Cyclic | Cyclic |
| N-terminal_Modification | Free |
| C-terminal_Modification | amide |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 2167.45 |
|---|---|
| Aliphatic_Index | 43.33333 |
| Aromaticity | 0.22222 |
| Average_Rotatable_Bonds | 3.50000 |
| Charge_at_pH_7 | -1.12198 |
| Isoelectric_Point | 4.42631 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 26 |
| Number_of_Hydrogen_Bond_Donors | 32 |
| Topological_Polar_Surface_Area | 832.30000 |
| X_logP_energy | -4.23256 |
Interaction Information
| Affinity | IC50=7 uM |
|---|---|
| Affinity_Assay | ELISA |
| PDB_ID | None |
| Type | antagonist |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress. |
| Release_Year | 2003 |
| PMID | None |
| DOI | 10.1155/2003/364613 |