PPIRE15825
Target Protein Information
| Protein_Name | Prolyl 4-hydroxylase subunit alpha-2 |
|---|---|
| Protein_Sequence | MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD |
| Organism_Source | Homo sapiens |
| Functional_Classification | prolyl 4 hydroxylases |
| Cellular_Localization | Extracellular |
| Gene_Names | P4HA2 |
| UniProt_ID | O15460 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | (Pro-Pro-Gly)10 |
|---|---|
| Peptide_Sequence | PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGPPG |
| Peptide_Length | 33 |
| Peptide_SMILES | O=C(O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1C(=O)CNC(=O)[C@@H]1CCCN1C(=O)[C@@H]1CCCN1 |
| Chemical_Modification | None |
| Cyclization_Method | None |
| Linear/Cyclic | Linear |
| N-terminal_Modification | Free |
| C-terminal_Modification | Free |
| Amino_Acid_Distribution | |
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Peptide Physicochemical
| Molecular_Weight | 2782.15 |
|---|---|
| Aliphatic_Index | 0.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 1.33333 |
| Charge_at_pH_7 | -0.00202 |
| Isoelectric_Point | 6.10000 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 34 |
| Number_of_Hydrogen_Bond_Donors | 13 |
| Topological_Polar_Surface_Area | 795.94000 |
| X_logP_energy | -10.08780 |
Interaction Information
| Affinity | Km=100 uM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | None |
| Type | Substrate |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | The Peptide-Substrate-binding Domain of Human Collagen Prolyl 4-Hydroxylases: Backbone Assignments Secondary Structure and Binding of Proline-Rich Peptides |
| Release_Year | 2003 |
| PMID | 12824157 |
| DOI | 10.1074/jbc.M303624200 |