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Yorodumi- PDB-1vfq: The Crystal Structure of Human Coactosin-like Protein at 1.9 A Re... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1vfq | ||||||
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Title | The Crystal Structure of Human Coactosin-like Protein at 1.9 A Resolution | ||||||
Components | Coactosin-like protein | ||||||
Keywords | PROTEIN BINDING / Cytoskeleton / Actin-binding protein | ||||||
Function / homology | Function and homology information site of polarized growth / regulation of actin filament polymerization / cortical actin cytoskeleton / defense response to fungus / actin filament binding / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation / enzyme binding ...site of polarized growth / regulation of actin filament polymerization / cortical actin cytoskeleton / defense response to fungus / actin filament binding / actin binding / secretory granule lumen / ficolin-1-rich granule lumen / Neutrophil degranulation / enzyme binding / extracellular exosome / extracellular region / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Li, X. / Liu, Y. / Liu, X. / Lou, Z. | ||||||
Citation | Journal: PROTEIN SCI. / Year: 2004 Title: Crystal structure of human coactosin-like protein at 1.9 A resolution Authors: Li, X. / Liu, X. / Lou, Z. / Duan, X. / Wu, H. / Liu, Y. / Rao, Z. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1vfq.cif.gz | 40 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1vfq.ent.gz | 27.1 KB | Display | PDB format |
PDBx/mmJSON format | 1vfq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/vf/1vfq ftp://data.pdbj.org/pub/pdb/validation_reports/vf/1vfq | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 16053.041 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pGEX-6p-1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q14019 |
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#2: 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: 1.6 Å3/Da / Density % sol: 24 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: 30% PEG4000, 0.1M Tris-HCL, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: AREA DETECTOR / Date: Jun 17, 2003 |
Radiation | Monochromator: osmic mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. all: 8223 / Num. obs: 7524 / % possible obs: 91.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.3 % / Biso Wilson estimate: 41.3 Å2 / Rmerge(I) obs: 0.262 / Net I/σ(I): 13.8 |
Reflection shell | Resolution: 1.9→1.97 Å / % possible all: 91.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→23.12 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.9→23.12 Å
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Refine LS restraints |
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