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Yorodumi- PDB-2p2t: Crystal structure of dynein light chain LC8 bound to residues 123... -
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-Basic information
Entry | Database: PDB / ID: 2p2t | ||||||
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Title | Crystal structure of dynein light chain LC8 bound to residues 123-138 of intermediate chain IC74 | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / protein - peptide complex | ||||||
Function / homology | Function and homology information cellularization / spermatid nucleus elongation / eye photoreceptor cell differentiation / chaeta morphogenesis / positive regulation of neuron remodeling / Macroautophagy / Aggrephagy / wing disc development / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-mediated anterograde transport ...cellularization / spermatid nucleus elongation / eye photoreceptor cell differentiation / chaeta morphogenesis / positive regulation of neuron remodeling / Macroautophagy / Aggrephagy / wing disc development / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / COPI-mediated anterograde transport / COPI-independent Golgi-to-ER retrograde traffic / transport along microtubule / : / chaeta development / sperm individualization / dynein light chain binding / microtubule anchoring at centrosome / imaginal disc-derived wing morphogenesis / dynein heavy chain binding / Neutrophil degranulation / dynein complex / cytoplasmic dynein complex / dynein light intermediate chain binding / protein localization to kinetochore / axo-dendritic transport / centrosome localization / spindle organization / dynein intermediate chain binding / oogenesis / microtubule-based movement / dynactin binding / establishment of mitotic spindle orientation / actin filament bundle assembly / centriole / microtubule cytoskeleton organization / autophagy / disordered domain specific binding / spermatogenesis / nuclear membrane / microtubule / molecular adaptor activity / neuron projection / lysosomal membrane / protein homodimerization activity / protein-containing complex / cytoplasm Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3 Å | ||||||
Authors | Benison, G. / Karplus, P.A. / Barbar, E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Structure and dynamics of LC8 complexes with KXTQT-motif peptides: swallow and dynein intermediate chain compete for a common site. Authors: Benison, G. / Karplus, P.A. / Barbar, E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2p2t.cif.gz | 53.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2p2t.ent.gz | 39.2 KB | Display | PDB format |
PDBx/mmJSON format | 2p2t.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p2/2p2t ftp://data.pdbj.org/pub/pdb/validation_reports/p2/2p2t | HTTPS FTP |
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-Related structure data
Related structure data | |
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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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Details | The biological assembly is a dimer generated from the monomer in the asymmetric unit by the operation: -y, -x, -z + 1/6 |
-Components
#1: Protein | Mass: 10388.849 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Gene: ctp, Cdlc1, ddlc1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q24117 |
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#2: Protein/peptide | Mass: 1787.961 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence of the peptide can be naturally found in Drosophila melanogaster (Fruit fly). References: UniProt: Q24246 |
#3: Chemical | ChemComp-ACT / |
#4: Chemical | ChemComp-NA / |
#5: 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: 2.38 Å3/Da / Density % sol: 48.41 % |
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-Data collection
Diffraction | Mean temperature: 130 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 13, 2006 |
Radiation | Monochromator: Ni filter / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→40 Å / Num. all: 2856 / Num. obs: 2817 / % possible obs: 98.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rsym value: 0.069 / Net I/σ(I): 30 |
Reflection shell | Resolution: 3→3.05 Å / Mean I/σ(I) obs: 12.5 / Num. unique all: 166 / Rsym value: 0.245 / % possible all: 94.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→22.18 Å / Cor.coef. Fo:Fc: 0.93 / Cor.coef. Fo:Fc free: 0.842 / SU B: 42.419 / SU ML: 0.404 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.534 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.159 Å2
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Refinement step | Cycle: LAST / Resolution: 3→22.18 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.077 Å / Total num. of bins used: 20
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