UniProt P31749
RAC-alpha serine/threonine-protein kinase (P31749)
RAC-alpha serine/threonine-protein kinase (UniProt P31749), EC 2.7.11.1: 56 experimental structures and 1 predicted model on GenesisL1, 13 ligands bound, 15 pockets. Binding sites, druggability and experiment against prediction…
- UniProt
- P31749
- Protein
- RAC-alpha serine/threonine-protein kinase
- EC
- 2.7.11.1
- Experimental structures
- 56
- Predicted models
- 1
- Ligands
- 13
- Pockets
- 15 · 2 records with a druggable one
Structures
57 records of P31749 in the MolNFT archive: 56 experimental, 1 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1H10 | High resolution structure of the pleckstrin homology domain of protein kinase B/AKT bound to… | x-ray diffraction | A | — | — |
| 1H10 | High resolution structure of the pleckstrin homology domain of protein kinase B/AKT bound to… | x-ray diffraction | A | — | — |
| 1UNP | Crystal structure of the pleckstrin homology domain of PKB alpha | x-ray diffraction | A | — | — |
| 1UNP | Crystal structure of the pleckstrin homology domain of pkb alpha | x-ray diffraction | A | — | — |
| 1UNQ | High resolution crystal structure of the Pleckstrin Homology Domain Of Protein Kinase B/Akt Bound… | x-ray diffraction | A | — | — |
| 1UNQ | High resolution crystal structure of the pleckstrin homology domain of protein kinase B/AKT bound… | x-ray diffraction | A | — | — |
| 1UNR | Crystal structure of the PH domain of PKB alpha in complex with a sulfate molecule | x-ray diffraction | A | — | — |
| 1UNR | Crystal structure of the pH domain of pkb alpha in complex with a sulfate molecule | x-ray diffraction | A | — | — |
| 2UVM | Structure of PKBalpha PH domain in complex with a novel inositol headgroup surrogate, benzene… | x-ray diffraction | A | — | — |
| 2UVM | Structure of pkbalpha pH domain in complex with a novel inositol headgroup surrogate, benzene… | x-ray diffraction | A | — | — |
| 2UZR | A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) | x-ray diffraction | A | — | — |
| 2UZR | A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) | x-ray diffraction | A | — | — |
| 2UZS | A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) | x-ray diffraction | A | — | — |
| 2UZS | A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) | x-ray diffraction | A | — | — |
| 3CQU | Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor | x-ray diffraction | A | — | — |
| 3CQU | Crystal structure of AKT-1 complexed with substrate peptide and inhibitor | x-ray diffraction | A | — | — |
| 3CQW | Crystal Structure of Akt-1 complexed with substrate peptide and inhibitor | x-ray diffraction | A | — | — |
| 3CQW | Crystal structure of AKT-1 complexed with substrate peptide and inhibitor | x-ray diffraction | A | — | — |
| 3O96 | Crystal Structure of Human AKT1 with an Allosteric Inhibitor | x-ray diffraction | A | — | — |
| 3O96 | Crystal structure of human AKT1 with an allosteric inhibitor | x-ray diffraction | A | — | — |
| 3OW4 | Discovery of dihydrothieno- and dihydrofuropyrimidines as potent pan Akt inhibitors | x-ray diffraction | A, B | — | — |
| 3OW4 | Discovery of dihydrothieno- and dihydrofuropyrimidines as potent pan AKT inhibitors | x-ray diffraction | A, B | — | — |
| 3QKK | Spirochromane Akt Inhibitors | x-ray diffraction | A | — | — |
| 3QKK | Spirochromane AKT inhibitors | x-ray diffraction | A | — | — |
| 3QKL | Spirochromane Akt Inhibitors | x-ray diffraction | A | — | — |
| 3QKL | Spirochromane AKT inhibitors | x-ray diffraction | A | — | — |
| 3QKM | Spirocyclic sulfonamides as AKT inhibitors | x-ray diffraction | A | — | — |
| 3QKM | Spirocyclic sulfonamides as AKT inhibitors | x-ray diffraction | A | — | — |
| 4EJN | Crystal structure of autoinhibited form of AKT1 in complex with… | x-ray diffraction | A | — | — |
| 4EJN | Crystal structure of autoinhibited form of AKT1 in complex with N-(4… | x-ray diffraction | A | — | — |
| 4EKK | Akt1 with AMP-PNP | x-ray diffraction | A, B | — | — |
| 4EKK | AKT1 with AMP-pnp | x-ray diffraction | A, B | — | — |
| 4EKL | Akt1 with GDC0068 | x-ray diffraction | A | — | — |
| 4EKL | AKT1 with GDC0068 | x-ray diffraction | A | — | — |
| 4GV1 | PKB alpha in complex with AZD5363 | x-ray diffraction | A | — | — |
| 4GV1 | Pkb alpha in complex with AZD5363 | x-ray diffraction | A | — | — |
| 5KCV | Crystal structure of allosteric inhibitor, ARQ 092, in complex with autoinhibited form of AKT1 | x-ray diffraction | A | 6S1 | — |
| 5KCV | Crystal structure of allosteric inhibitor, arq 092, in complex with autoinhibited form of AKT1 | x-ray diffraction | A | 6S1 | — |
| 6BUU | Crystal structure of AKT1 (aa 144-480) with a bisubstrate | x-ray diffraction | A, B | SO4, MN | 9 (best 0.75) |
| 6BUU | Crystal structure of AKT1 (aa 144-480) with a bisubstrate | x-ray diffraction | A, B | SO4, MN | — |
| 6CCY | Crystal structure of AKT1 in complex with a selective inhibitor | x-ray diffraction | A | EX4 | — |
| 6HHF | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor borussertib | x-ray diffraction | A | G4K | — |
| 6HHG | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 27 | x-ray diffraction | A | G4T | — |
| 6HHH | Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 31 | x-ray diffraction | A | G4Q | — |
| 6HHH | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 31 | x-ray diffraction | A | G4Q | — |
| 6HHI | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 30B | x-ray diffraction | A | G4N | — |
| 6HHJ | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 24B | x-ray diffraction | A | G4H | — |
| 6NPZ | Crystal structure of Akt1 (aa 123-480) kinase with a bisubstrate | x-ray diffraction | A, B | MN | — |
| 6NPZ | Crystal structure of AKT1 (aa 123-480) kinase with a bisubstrate | x-ray diffraction | A, B | MN | — |
| 6S9W | Crystal Structure of AKT1 in Complex with Covalent-Allosteric AKT Inhibitor 16a | x-ray diffraction | A | L1Z | — |
| 6S9W | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 16A | x-ray diffraction | A | L1Z | — |
| 6S9X | Crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 15C | x-ray diffraction | A | L1W | — |
| 7APJ | Structure of autoinhibited Akt1 reveals mechanism of PIP3-mediated activation | x-ray diffraction | A | — | 6 (best 0.52) |
| 7APJ | Structure of autoinhibited AKT1 reveals mechanism of PIP3-mediated activation | x-ray diffraction | A | — | — |
| 7NH4 | Co-crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 3 | x-ray diffraction | A | UCE | — |
| 7NH5 | Co-crystal structure of AKT1 in complex with covalent-allosteric AKT inhibitor 6 | x-ray diffraction | A | UC8 | — |
| P31749 | AlphaFold monomer V2.0 prediction for rac-alpha SERINE/THREONINE- protein kinase (P31749) | predicted | A | — | — |
Ligands
- MN · Manganese (II) ion · in 4 records
- 6S1 · 3-[3-[4-(1-azanylcyclobutyl)phenyl]-5-phenyl-imidazo[4, 5-b]pyridin-2-yl]pyridin-2-amine · in 2 records
- G4Q · ~{N}-[4-[4-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperazin-1-yl]phenyl]propanamide · in 2 records
- L1Z · ~{N}-[3-[1-[[4-(5-methyl-6-oxidanylidene-3-phenyl-1~{H}-pyrazin-2-yl)phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide · in 2 records
- SO4 · Sulfate ion · in 2 records
- EX4 · (5R)-4-(4-{4-[4-fluoro-3-(trifluoromethyl)phenyl]-1-[2-(pyrrolidin-1-yl)ethyl]-1H-imidazol-2-yl}piperidin-1-yl)-5-methyl-5,8-dihydropyrido[2,3-d]pyrimidin-7(6H)-one · in 1 record
- G4H · ~{N}-[1-methyl-2-oxidanylidene-3-[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl) phenyl]methyl]piperidin-4-yl]benzimidazol-5-yl]propanamide · in 1 record
- G4K · Borussertib · in 1 record
- G4N · ~{N}-[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperidin-4-yl]-3-(propanoylamino)benzamide · in 1 record
- G4T · ~{N}-[2-chloranyl-5-[[1-[[4-(5-oxidanylidene-3-phenyl-6~{H}-1,6-naphthyridin-2-yl)phenyl]methyl]piperidin-4-yl]carbamoylamino]phenyl]propanamide · in 1 record
- L1W · ~{N}-[3-[1-[[4-[5-[(4-hydroxyphenyl)methyl]-6-oxidanylidene-2-phenyl-1~{H}-pyrazin-3-yl]phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide · in 1 record
- UC8 · ~{N}-methyl-6-[4-[[4-[2-oxidanylidene-6-(propanoylamino)-3~{H}-benzimidazol-1-yl]piperidin-1-yl]methyl]phenyl]-5-phenyl-pyridine-3-carboxamide · in 1 record
- UCE · ~{N}-[3-[1-[[4-[5-(hydroxymethyl)-3-phenyl-pyridin-2-yl]phenyl]methyl]piperidin-4-yl]-2-oxidanylidene-1~{H}-benzimidazol-5-yl]propanamide · in 1 record
Experiment against prediction
- 4EKK chain A against the predicted model P31749: TM-score 0.98, RMSD 1.25 Å
- 4EKK chain A against the predicted model P31749: TM-score 0.98, RMSD 1.25 Å
- 3OW4 chain B against the predicted model P31749: TM-score 0.98, RMSD 1.09 Å
- 3OW4 chain B against the predicted model P31749: TM-score 0.98, RMSD 1.09 Å
- 3OW4 chain A against the predicted model P31749: TM-score 0.98, RMSD 1.12 Å
- 3OW4 chain A against the predicted model P31749: TM-score 0.98, RMSD 1.12 Å
- 3CQW chain A against the predicted model P31749: TM-score 0.98, RMSD 1.23 Å
- 3CQW chain A against the predicted model P31749: TM-score 0.98, RMSD 1.23 Å
- 6BUU chain B against the predicted model P31749: TM-score 0.98, RMSD 1.24 Å
- 6BUU chain B against the predicted model P31749: TM-score 0.98, RMSD 1.24 Å
Elsewhere
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