PPIRE04094
Target Protein Information
| Protein_Name | None |
|---|---|
| Protein_Sequence | MSKDVSSTITTVSASPDGTLNLPAAAPLSIASGRLNQTILETGSQFGGVARWGQESHEFGMRRLAGTALDGAMRDWFTNECESLGCKVKVDKIGNMFAVYPGKNGGKPTATGSHLDTQPEAGKYDGILGVLAGLEVLRTFKDNNYVPNYDVCVVVWFNEEGARFARSCTGSSVWSHDLSLEEAYGLMSVGEDKPESVYDSLKNIGYIGDTPASYKENEIDAHFELHIEQGPILEDENKAIGIVTGVQAYNWQKVTVHGVGAHAGTTPWRLRKDALLMSSKMIVAASEIAQRHNGLFTCGIIDAKPYSVNIIPGEVSFTLDFRHPSDDVLATMLKEAAAEFDRLIKINDGGALSYESETLQVSPAVNFHEVCIECVSRSAFAQFKKDQVRQIWSGAGHDSCQTAPHVPTSMIFIPSKDGLSHNYYEYSSPEEIENGFKVLLQAIINYDNYRVIRGH |
| Organism_Source | Lachancea kluyveri |
| Functional_Classification | amidohydrolases |
| Cellular_Localization | Cytoplasm |
| Gene_Names | PYD3 |
| UniProt_ID | Q96W94 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Gly-Gly |
|---|---|
| Peptide_Sequence | GG |
| Peptide_Length | 2 |
| Peptide_SMILES | NCC(=O)NCC(=O)O |
| 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 | 132.12 |
|---|---|
| Aliphatic_Index | 0.00000 |
| Aromaticity | 0.00000 |
| Average_Rotatable_Bonds | 1.50000 |
| Charge_at_pH_7 | -0.00202 |
| Isoelectric_Point | 6.10000 |
|---|---|
| Number_of_Hydrogen_Bond_Acceptors | 3 |
| Number_of_Hydrogen_Bond_Donors | 3 |
| Topological_Polar_Surface_Area | 92.42000 |
| X_logP_energy | -1.85410 |
Interaction Information
| Affinity | Ki=45 mM |
|---|---|
| Affinity_Assay | Enzyme Inhibition Kinetics |
| PDB_ID | 2VL1 |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | A recruited protease is involved in catabolism of pyrimidines. |
| Release_Year | 2008 |
| PMID | 18448119 |
| DOI | 10.1016/j.jmb.2008.03.073 |