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Yorodumi- PDB-2uzr: A transforming mutation in the pleckstrin homology domain of AKT1... -
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-Basic information
Entry | Database: PDB / ID: 2uzr | ||||||
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Title | A transforming mutation in the pleckstrin homology domain of AKT1 in cancer (AKT1-PH_E17K) | ||||||
Components | RAC-alpha serine/threonine-protein kinase | ||||||
Keywords | TRANSFERASE / GLYCOGEN BIOSYNTHESIS / TRANSLATION REGULATION / NUCLEOTIDE- BINDING / GLYCOGEN METABOLISM / ATP-BINDING / SUGAR TRANSPORT / NUCLEAR PROTEIN / SERINE/THREONINE-PROTEIN KINASE / TRANSPORT / CARBOHYDRATE METABOLISM / KINASE / APOPTOSIS / PHOSPHORYLATION / GLUCOSE METABOLISM | ||||||
Function / homology | Function and homology information glycogen cell differentiation involved in embryonic placenta development / regulation of tRNA methylation / response to insulin-like growth factor stimulus / potassium channel activator activity / negative regulation of protein localization to lysosome / positive regulation of protein localization to endoplasmic reticulum / maintenance of protein location in mitochondrion / negative regulation of lymphocyte migration / cellular response to decreased oxygen levels / regulation of type B pancreatic cell development ...glycogen cell differentiation involved in embryonic placenta development / regulation of tRNA methylation / response to insulin-like growth factor stimulus / potassium channel activator activity / negative regulation of protein localization to lysosome / positive regulation of protein localization to endoplasmic reticulum / maintenance of protein location in mitochondrion / negative regulation of lymphocyte migration / cellular response to decreased oxygen levels / regulation of type B pancreatic cell development / AKT-mediated inactivation of FOXO1A / maternal placenta development / Negative regulation of the PI3K/AKT network / negative regulation of long-chain fatty acid import across plasma membrane / establishment of protein localization to mitochondrion / negative regulation of fatty acid beta-oxidation / regulation of glycogen biosynthetic process / AKT phosphorylates targets in the nucleus / cellular response to oxidised low-density lipoprotein particle stimulus / negative regulation of cilium assembly / positive regulation of I-kappaB phosphorylation / Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA / response to fluid shear stress / RUNX2 regulates genes involved in cell migration / positive regulation of organ growth / MTOR signalling / fibroblast migration / interleukin-18-mediated signaling pathway / positive regulation of sodium ion transport / mammary gland epithelial cell differentiation / negative regulation of endopeptidase activity / negative regulation of protein serine/threonine kinase activity / mammalian oogenesis stage / RAB GEFs exchange GTP for GDP on RABs / positive regulation of glucose metabolic process / positive regulation of endodeoxyribonuclease activity / positive regulation of protein localization to cell surface / protein serine/threonine kinase inhibitor activity / cellular response to granulocyte macrophage colony-stimulating factor stimulus / response to growth factor / activation-induced cell death of T cells / negative regulation of leukocyte cell-cell adhesion / phosphatidylinositol-3,4-bisphosphate binding / peripheral nervous system myelin maintenance / sphingosine-1-phosphate receptor signaling pathway / glycogen biosynthetic process / positive regulation of fibroblast migration / cell migration involved in sprouting angiogenesis / anoikis / response to growth hormone / AKT phosphorylates targets in the cytosol / execution phase of apoptosis / labyrinthine layer blood vessel development / response to food / response to UV-A / regulation of myelination / regulation of postsynapse organization / regulation of neuron projection development / KSRP (KHSRP) binds and destabilizes mRNA / Regulation of TP53 Activity through Association with Co-factors / negative regulation of macroautophagy / CTLA4 inhibitory signaling / negative regulation of cGAS/STING signaling pathway / negative regulation of Notch signaling pathway / behavioral response to pain / negative regulation of release of cytochrome c from mitochondria / Constitutive Signaling by AKT1 E17K in Cancer / non-canonical NF-kappaB signal transduction / apoptotic mitochondrial changes / CD28 dependent PI3K/Akt signaling / phosphatidylinositol-3,4,5-trisphosphate binding / carbohydrate transport / Regulation of localization of FOXO transcription factors / positive regulation of cyclin-dependent protein serine/threonine kinase activity / TOR signaling / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / positive regulation of glycogen biosynthetic process / Activation of BAD and translocation to mitochondria / positive regulation of fat cell differentiation / positive regulation of blood vessel endothelial cell migration / canonical NF-kappaB signal transduction / cellular response to vascular endothelial growth factor stimulus / positive regulation of G1/S transition of mitotic cell cycle / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / eNOS activation / Cyclin E associated events during G1/S transition / positive regulation of lipid biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / Cyclin A:Cdk2-associated events at S phase entry / Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation / lipopolysaccharide-mediated signaling pathway / regulation of cell migration / negative regulation of protein ubiquitination / cellular response to epidermal growth factor stimulus / 14-3-3 protein binding / Regulation of TP53 Activity through Acetylation / positive regulation of endothelial cell proliferation / positive regulation of TORC1 signaling / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.94 Å | ||||||
Authors | Carpten, J.D. / Faber, A.L. / Horn, C. / Donoho, G.P. / Briggs, S.L. / Robbins, C.M. / Hostetter, G. / Boguslawski, S. / Moses, T.Y. / Savage, S. ...Carpten, J.D. / Faber, A.L. / Horn, C. / Donoho, G.P. / Briggs, S.L. / Robbins, C.M. / Hostetter, G. / Boguslawski, S. / Moses, T.Y. / Savage, S. / Uhlik, M. / Lin, A. / Du, J. / Qian, Y.W. / Zeckner, D.J. / Tucker-Kellogg, G. / Touchman, J. / Patel, K. / Mousses, S. / Bittner, M. / Schevitz, R. / Lai, M.H. / Blanchard, K.L. / Thomas, J.E. | ||||||
Citation | Journal: Nature / Year: 2007 Title: A transforming mutation in the pleckstrin homology domain of AKT1 in cancer. Authors: Carpten, J.D. / Faber, A.L. / Horn, C. / Donoho, G.P. / Briggs, S.L. / Robbins, C.M. / Hostetter, G. / Boguslawski, S. / Moses, T.Y. / Savage, S. / Uhlik, M. / Lin, A. / Du, J. / Qian, Y.W. ...Authors: Carpten, J.D. / Faber, A.L. / Horn, C. / Donoho, G.P. / Briggs, S.L. / Robbins, C.M. / Hostetter, G. / Boguslawski, S. / Moses, T.Y. / Savage, S. / Uhlik, M. / Lin, A. / Du, J. / Qian, Y.W. / Zeckner, D.J. / Tucker-Kellogg, G. / Touchman, J. / Patel, K. / Mousses, S. / Bittner, M. / Schevitz, R. / Lai, M.H. / Blanchard, K.L. / Thomas, J.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2uzr.cif.gz | 38.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2uzr.ent.gz | 25.3 KB | Display | PDB format |
PDBx/mmJSON format | 2uzr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uz/2uzr ftp://data.pdbj.org/pub/pdb/validation_reports/uz/2uzr | HTTPS FTP |
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-Related structure data
Related structure data | 2uzsC 1unqS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 14773.732 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-123 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: AKT1, PKB, RAC / Cell line (production host): HEK293T / Production host: Homo sapiens (human) References: UniProt: P31749, non-specific serine/threonine protein kinase | ||
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#2: Water | ChemComp-HOH / | ||
Compound details | ENGINEEREDSequence details | MUTATED E17K | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.7 Å3/Da / Density % sol: 28.27 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: 0.1 M HEPES PH 7.5 AND 1.4 M SODIUM CITRATE, OR 0.1 M SODIUM ACETATE PH 4.6, 0.2 M AMMONIUM ACETATE AND 15%-30% PEG 3350, |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 17, 2006 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.94→36.64 Å / Num. obs: 7529 / % possible obs: 97.1 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 4.9 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 2 % / Rmerge(I) obs: 0.139 / Mean I/σ(I) obs: 2.11 / % possible all: 86.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1UNQ Resolution: 1.94→36.64 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.915 / SU B: 4.931 / SU ML: 0.146 / Cross valid method: THROUGHOUT / ESU R: 0.276 / ESU R Free: 0.194 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. RESIDUES 43-47 ARE DISORDERED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.96 Å2
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Refinement step | Cycle: LAST / Resolution: 1.94→36.64 Å
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Refine LS restraints |
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