PPIRE17974
Target Protein Information
| Protein_Name | Adenylate kinase isoenzyme 1 |
|---|---|
| Protein_Sequence | MEEKLKKAKIIFVVGGPGSGKGTQCEKIVHKYGYTHLSTGDLLRAEVSSGSARGKKLSEIMEKGQLVPLETVLDMLRDAMVAKADTSKGFLIDGYPRQVQQGEEFERRIAQPTLLLYVDAGPETMQKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKVNAEGSVDNVFSQVCTHLDALK |
| Organism_Source | Oryctolagus cuniculus |
| Functional_Classification | kinases |
| Cellular_Localization | Cytoplasm |
| Gene_Names | AK1 |
| UniProt_ID | P00569 |
| Protein-Protein Interaction Networks | |
Peptide Basic Information
| Peptide_Name | Rabbit muscle adenylate kinase peptide fragment (residues 1-45) |
|---|---|
| Peptide_Sequence | MEEKLKKAKIDIVFVVGGPGSGKSTQCEKIVHGLEEFGKNLDTET |
| Peptide_Length | 45 |
| Peptide_SMILES | CC[C@H](C)[C@H](NC(=O)[C@H](CCCCN)NC(=O)[C@H](C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@@H](N)CCSC)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](Cc1ccccc1)C(=O)N[C@H](C(=O)N[C@H](C(=O)NCC(=O)NCC(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CO)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@H](C(=O)N[C@H](C(=O)N[C@@H](Cc1c[nH]cn1)C(=O)NCC(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@@H](Cc1ccccc1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(=O)O)C(=O)N[C@H](C(=O)N[C@@H](CCC(=O)O)C(=O)N[C@H](C(=O)O)[C@@H](C)O)[C@@H](C)O)C(C)C)[C@@H](C)CC)[C@@H](C)O)C(C)C)C(C)C)C(C)C)[C@@H](C)CC |
| 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 | 4891.63 |
|---|---|
| Aliphatic_Index | 80.00000 |
| Aromaticity | 0.04444 |
| Average_Rotatable_Bonds | 3.86667 |
| Charge_at_pH_7 | -0.96360 |
| Isoelectric_Point | 5.76784 |
|---|---|
| Hydrogen_Bond_Acceptors | 71 |
| Hydrogen_Bond_Donors | 69 |
| Topological_Polar_Surface_Area | 2031.48000 |
| X_logP_energy | -19.61220 |
Interaction Information
| Affinity | KD=35 uM |
|---|---|
| Affinity_Assay | NMR chemical shift perturbation |
| PDB_ID | None |
| Type | Inhibitor |
| Structure | |
Reference Information
| Document_Type | Research Articles |
|---|---|
| Title | NMR Studies of the MgATP Binding Site of Adenylate Kinase and of a 45-Residue Peptide Fragment of the Enzyme |
| Release_Year | 1985 |
| PMID | 2862911 |
| DOI | 10.1021/bi00334a015 |