+Open data
-Basic information
Entry | Database: PDB / ID: 6fdz | ||||||
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Title | Unc-51-Like Kinase 3 (ULK3) In Complex With Momelotinib | ||||||
Components | Serine/threonine-protein kinase ULK3 | ||||||
Keywords | TRANSFERASE / Kinase Inhibitor DFG-out | ||||||
Function / homology | Function and homology information ciliary tip / phagophore assembly site membrane / piecemeal microautophagy of the nucleus / fibroblast activation / positive regulation of smoothened signaling pathway / phagophore assembly site / reticulophagy / smoothened signaling pathway / response to starvation / autophagosome assembly ...ciliary tip / phagophore assembly site membrane / piecemeal microautophagy of the nucleus / fibroblast activation / positive regulation of smoothened signaling pathway / phagophore assembly site / reticulophagy / smoothened signaling pathway / response to starvation / autophagosome assembly / autophagosome / negative regulation of smoothened signaling pathway / regulation of autophagy / Hedgehog 'on' state / autophagy / cellular senescence / protein autophosphorylation / non-specific serine/threonine protein kinase / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å | ||||||
Authors | Mathea, S. / Salah, E. / Moroglu, M. / Scorah, A. / Pike, A.C.W. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Huber, K. / Knapp, S. | ||||||
Citation | Journal: To Be Published Title: Unc-51-Like Kinase 3 (ULK3) In Complex With Momelotinib Authors: Mathea, S. / Salah, E. / Moroglu, M. / Scorah, A. / von Delft, F. / Arrowsmith, C.H. / Edwards, A.M. / Bountra, C. / Huber, K. / Knapp, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6fdz.cif.gz | 67 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6fdz.ent.gz | 47.7 KB | Display | PDB format |
PDBx/mmJSON format | 6fdz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fd/6fdz ftp://data.pdbj.org/pub/pdb/validation_reports/fd/6fdz | HTTPS FTP |
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-Related structure data
Related structure data | 4wnpS 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: 31939.977 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ULK3 / Production host: Spodoptera frugiperda (fall armyworm) References: UniProt: Q6PHR2, non-specific serine/threonine protein kinase |
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#2: Chemical | ChemComp-C87 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.91 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.1 M HEPES pH 7.5, 0.2 M MgCl2, 30% 2-propanol |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I24 / Wavelength: 0.9686 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 6, 2017 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9686 Å / Relative weight: 1 |
Reflection | Resolution: 2.55→214.69 Å / Num. obs: 12814 / % possible obs: 100 % / Redundancy: 18.7 % / Rrim(I) all: 0.14 / Net I/σ(I): 17 |
Reflection shell | Resolution: 2.55→2.59 Å / Redundancy: 19.7 % / Mean I/σ(I) obs: 2.2 / Num. unique obs: 608 / Rrim(I) all: 1.636 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4wnp Resolution: 2.55→65.68 Å / Cor.coef. Fo:Fc: 0.93 / Cor.coef. Fo:Fc free: 0.897 / SU B: 10.806 / SU ML: 0.238 / Cross valid method: THROUGHOUT / ESU R: 0.435 / ESU R Free: 0.321 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 58.642 Å2
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Refinement step | Cycle: 1 / Resolution: 2.55→65.68 Å
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Refine LS restraints |
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