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- PDB-6qdl: Molecular features of the UNC-45 chaperone critical for binding a... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6qdl | ||||||
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Title | Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin | ||||||
![]() | UNC-45 | ||||||
![]() | CHAPERONE / MYOSIN FOLDING / PROTEIN FILAMENTS / MYOFILAMENT FORMATION | ||||||
Function / homology | ![]() egg-laying behavior / locomotion / embryo development ending in birth or egg hatching / muscle organ development / sarcomere organization / cleavage furrow / chaperone-mediated protein folding / protein folding chaperone / Hsp90 protein binding / cell cortex ...egg-laying behavior / locomotion / embryo development ending in birth or egg hatching / muscle organ development / sarcomere organization / cleavage furrow / chaperone-mediated protein folding / protein folding chaperone / Hsp90 protein binding / cell cortex / ubiquitin protein ligase binding / perinuclear region of cytoplasm / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Meinhart, A. / Clausen, T. / Hellerschmied, D. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin. Authors: Hellerschmied, D. / Lehner, A. / Franicevic, N. / Arnese, R. / Johnson, C. / Vogel, A. / Meinhart, A. / Kurzbauer, R. / Deszcz, L. / Gazda, L. / Geeves, M. / Clausen, T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 181.7 KB | Display | ![]() |
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PDB format | ![]() | 142.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.5 KB | Display | ![]() |
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Full document | ![]() | 432.1 KB | Display | |
Data in XML | ![]() | 29.4 KB | Display | |
Data in CIF | ![]() | 40.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6qdjC ![]() 6qdkC ![]() 6qdmC ![]() 4i2zS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 107602.109 Da / Num. of mol.: 1 / Mutation: I822F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 47.09 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 100 mM MES/NaOH pH 6.5 200 mM ammonium acetate 30 % glycerol ethoxylate |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 21, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9792 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→47 Å / Num. obs: 20543 / % possible obs: 97 % / Redundancy: 3.1 % / Rrim(I) all: 0.119 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 2.9→3.09 Å / Redundancy: 2.7 % / Mean I/σ(I) obs: 1.4 / Rrim(I) all: 0.675 / % possible all: 82.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4i2z Resolution: 2.929→46.704 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.8
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.929→46.704 Å
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Refine LS restraints |
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LS refinement shell |
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