+Open data
-Basic information
Entry | Database: PDB / ID: 1q3w | ||||||
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Title | GSK-3 Beta complexed with Alsterpaullone | ||||||
Components | GLYCOGEN SYNTHASE KINASE-3 BETA | ||||||
Keywords | TRANSFERASE / KINASE / INSULIN PATHWAY / ALSTERPAULLONE | ||||||
Function / homology | Function and homology information regulation of microtubule anchoring at centrosome / negative regulation of mesenchymal stem cell differentiation / negative regulation of glycogen (starch) synthase activity / beta-catenin destruction complex disassembly / neuron projection organization / negative regulation of type B pancreatic cell development / superior temporal gyrus development / : / positive regulation of protein localization to cilium / negative regulation of glycogen biosynthetic process ...regulation of microtubule anchoring at centrosome / negative regulation of mesenchymal stem cell differentiation / negative regulation of glycogen (starch) synthase activity / beta-catenin destruction complex disassembly / neuron projection organization / negative regulation of type B pancreatic cell development / superior temporal gyrus development / : / positive regulation of protein localization to cilium / negative regulation of glycogen biosynthetic process / negative regulation of dopaminergic neuron differentiation / positive regulation of protein localization to centrosome / maintenance of cell polarity / positive regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway / positive regulation of cilium assembly / negative regulation of protein acetylation / APC truncation mutants have impaired AXIN binding / AXIN missense mutants destabilize the destruction complex / Truncations of AMER1 destabilize the destruction complex / beta-catenin destruction complex / tau-protein kinase / CRMPs in Sema3A signaling / heart valve development / regulation of protein export from nucleus / regulation of microtubule-based process / Beta-catenin phosphorylation cascade / Signaling by GSK3beta mutants / CTNNB1 S33 mutants aren't phosphorylated / CTNNB1 S37 mutants aren't phosphorylated / CTNNB1 S45 mutants aren't phosphorylated / CTNNB1 T41 mutants aren't phosphorylated / Maturation of nucleoprotein / cellular response to interleukin-3 / negative regulation of TOR signaling / Wnt signalosome / negative regulation of protein localization to nucleus / regulation of long-term synaptic potentiation / Disassembly of the destruction complex and recruitment of AXIN to the membrane / Maturation of nucleoprotein / AKT phosphorylates targets in the cytosol / negative regulation of epithelial to mesenchymal transition / negative regulation of calcineurin-NFAT signaling cascade / positive regulation of cell-matrix adhesion / regulation of axon extension / G protein-coupled dopamine receptor signaling pathway / glycogen metabolic process / establishment of cell polarity / tau-protein kinase activity / regulation of axonogenesis / regulation of dendrite morphogenesis / ER overload response / regulation of neuron projection development / protein kinase A catalytic subunit binding / Constitutive Signaling by AKT1 E17K in Cancer / dynactin binding / NF-kappaB binding / Transcriptional and post-translational regulation of MITF-M expression and activity / Regulation of HSF1-mediated heat shock response / epithelial to mesenchymal transition / negative regulation of osteoblast differentiation / canonical Wnt signaling pathway / negative regulation of protein-containing complex assembly / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / regulation of microtubule cytoskeleton organization / positive regulation of autophagy / cellular response to retinoic acid / regulation of cellular response to heat / extrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / presynaptic modulation of chemical synaptic transmission / positive regulation of protein export from nucleus / positive regulation of GTPase activity / excitatory postsynaptic potential / negative regulation of cell migration / positive regulation of protein ubiquitination / mitochondrion organization / Ubiquitin-dependent degradation of Cyclin D / positive regulation of cell differentiation / hippocampus development / peptidyl-threonine phosphorylation / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / positive regulation of protein-containing complex assembly / negative regulation of canonical Wnt signaling pathway / Degradation of beta-catenin by the destruction complex / tau protein binding / B-WICH complex positively regulates rRNA expression / regulation of circadian rhythm / beta-catenin binding / circadian rhythm / positive regulation of protein catabolic process / cellular response to amyloid-beta / Regulation of RUNX2 expression and activity / neuron projection development / p53 binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of protein binding / insulin receptor signaling pathway / presynapse Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Bertrand, J.A. / Thieffine, S. / Vulpetti, A. / Cristiani, C. / Valsasina, B. / Knapp, S. / Kalisz, H.M. / Flocco, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Structural Characterization of the Gsk-3Beta Active Site Using Selective and Non-selective ATP-Mimetic Inhibitors Authors: Bertrand, J.A. / Thieffine, S. / Vulpetti, A. / Cristiani, C. / Valsasina, B. / Knapp, S. / Kalisz, H.M. / Flocco, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1q3w.cif.gz | 151.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1q3w.ent.gz | 118 KB | Display | PDB format |
PDBx/mmJSON format | 1q3w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1q3w_validation.pdf.gz | 974.9 KB | Display | wwPDB validaton report |
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Full document | 1q3w_full_validation.pdf.gz | 991.4 KB | Display | |
Data in XML | 1q3w_validation.xml.gz | 28 KB | Display | |
Data in CIF | 1q3w_validation.cif.gz | 38.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q3/1q3w ftp://data.pdbj.org/pub/pdb/validation_reports/q3/1q3w | HTTPS FTP |
-Related structure data
Related structure data | 1pyxC 1q3dC 1q41C 1q4lC 1h8fS C: citing same article (ref.) S: Starting model for refinement |
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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: 47081.473 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GSK3B / Plasmid: PVL-GST-GSK3BETA / Cell line (production host): H5 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P49841, EC: 2.7.1.37 #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.36 Å3/Da / Density % sol: 63.4 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 3350 MONODISPERSE, GLYCEROL, MAGNESIUM CHLORIDE, HEPES, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.2 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.933 / Wavelength: 0.933 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 6, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→30 Å / Num. obs: 57037 / % possible obs: 99.6 % / Redundancy: 3.414 % / Biso Wilson estimate: 27.7 Å2 / Rsym value: 0.06 / Net I/σ(I): 18.1086 |
Reflection shell | Resolution: 2.3→2.38 Å / Mean I/σ(I) obs: 2.367 / Rsym value: 0.512 / % possible all: 99.9 |
Reflection | *PLUS Highest resolution: 2.3 Å / Num. measured all: 194732 / Rmerge(I) obs: 0.06 |
Reflection shell | *PLUS % possible obs: 99.9 % / Rmerge(I) obs: 0.512 / Mean I/σ(I) obs: 2.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1H8F Resolution: 2.3→20.01 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2083785.5 / Data cutoff high rms absF: 2083785.5 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.1474 Å2 / ksol: 0.339746 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 52 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→20.01 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.44 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 30 Å | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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