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Yorodumi- PDB-2rjx: Crystal structure of the headpiece domain of chicken villin, P61 ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2rjx | ||||||
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Title | Crystal structure of the headpiece domain of chicken villin, P61 space group | ||||||
Components | Villin-1 | ||||||
Keywords | STRUCTURAL PROTEIN / HELIX / Actin capping / Actin-binding / Calcium / Cytoplasm / Cytoskeleton | ||||||
Function / homology | Function and homology information regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / positive regulation of actin filament bundle assembly / filopodium tip / actin filament severing / regulation of wound healing / actin filament capping / barbed-end actin filament capping ...regulation of actin nucleation / cytoplasmic actin-based contraction involved in cell motility / lysophosphatidic acid binding / regulation of lamellipodium morphogenesis / positive regulation of actin filament bundle assembly / filopodium tip / actin filament severing / regulation of wound healing / actin filament capping / barbed-end actin filament capping / actin filament depolymerization / actin polymerization or depolymerization / cellular response to hepatocyte growth factor stimulus / positive regulation of epithelial cell migration / actin filament bundle / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / microvillus / cellular response to epidermal growth factor stimulus / ruffle / phosphatidylinositol-4,5-bisphosphate binding / actin filament polymerization / filopodium / response to bacterium / epidermal growth factor receptor signaling pathway / actin filament binding / actin cytoskeleton / lamellipodium / regulation of cell shape / positive regulation of cell migration / calcium ion binding / protein homodimerization activity / cytoplasm Similarity search - Function | ||||||
Biological species | Gallus gallus (chicken) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.7 Å | ||||||
Authors | Meng, J. / Mcknight, C.J. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2009 Title: Heterogeneity and dynamics in villin headpiece crystal structures. Authors: Meng, J. / McKnight, C.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2rjx.cif.gz | 39.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2rjx.ent.gz | 27.8 KB | Display | PDB format |
PDBx/mmJSON format | 2rjx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rj/2rjx ftp://data.pdbj.org/pub/pdb/validation_reports/rj/2rjx | HTTPS FTP |
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-Related structure data
Related structure data | 2rjwC 1yu5S 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 7611.663 Da / Num. of mol.: 2 / Fragment: VILLIN HEADPIECE Source method: isolated from a genetically manipulated source Source: (gene. exp.) Gallus gallus (chicken) / Gene: VIL1, VIL / Plasmid: PVHP / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P02640 #2: 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: 2.68 Å3/Da / Density % sol: 54.17 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 8000, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 1, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→100 Å / Num. obs: 17717 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 10.8 % / Biso Wilson estimate: 31.2 Å2 / Rsym value: 0.038 / Net I/σ(I): 59 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 10.4 % / Mean I/σ(I) obs: 8.5 / Rsym value: 0.289 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1YU5 Resolution: 1.7→55.67 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 876432.95 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.17 Å2 / ksol: 0.37 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 28.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.7→55.67 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.7→1.81 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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