+Open data
-Basic information
Entry | Database: PDB / ID: 1dfc | ||||||
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Title | CRYSTAL STRUCTURE OF HUMAN FASCIN, AN ACTIN-CROSSLINKING PROTEIN | ||||||
Components | FASCIN | ||||||
Keywords | STRUCTURAL PROTEIN / BETA-TREFOIL FOLD FOR ALL FOUR DOMAINS / Structural Genomics / PSI / Protein Structure Initiative / New York SGX Research Center for Structural Genomics / NYSGXRC | ||||||
Function / homology | Function and homology information microspike / parallel actin filament bundle assembly / regulation of microvillus assembly / positive regulation of extracellular matrix disassembly / establishment of apical/basal cell polarity / microspike assembly / cell projection membrane / podosome / positive regulation of podosome assembly / cell-cell junction assembly ...microspike / parallel actin filament bundle assembly / regulation of microvillus assembly / positive regulation of extracellular matrix disassembly / establishment of apical/basal cell polarity / microspike assembly / cell projection membrane / podosome / positive regulation of podosome assembly / cell-cell junction assembly / positive regulation of filopodium assembly / establishment or maintenance of cell polarity / actin filament bundle assembly / microvillus / positive regulation of lamellipodium assembly / stress fiber / ruffle / filopodium / cell motility / regulation of actin cytoskeleton organization / cell-cell junction / actin filament binding / actin cytoskeleton / cell migration / lamellipodium / protein-macromolecule adaptor activity / actin binding / cell cortex / actin cytoskeleton organization / growth cone / Interleukin-4 and Interleukin-13 signaling / cytoskeleton / cadherin binding / RNA binding / extracellular exosome / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MIR / Resolution: 2.9 Å | ||||||
Authors | Fedorov, A.A. / Fedorov, E.V. / Ono, S. / Matsumura, F. / Almo, S.C. / Burley, S.K. / New York SGX Research Center for Structural Genomics (NYSGXRC) | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2010 Title: Structure, evolutionary conservation, and conformational dynamics of Homo sapiens fascin-1, an F-actin crosslinking protein. Authors: Sedeh, R.S. / Fedorov, A.A. / Fedorov, E.V. / Ono, S. / Matsumura, F. / Almo, S.C. / Bathe, M. #1: Journal: J.Biol.Chem. / Year: 1997 Title: Identification of an Actin Binding Region and a Protein Kinase C Phosphorylation Site on Human Fascin Authors: Ono, S. / Yamakita, Y. / Yamashiro, S. / Matsudaira, P.T. / Gnarra, J.R. / Obinata, T. / Matsumura, F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dfc.cif.gz | 193.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dfc.ent.gz | 155.2 KB | Display | PDB format |
PDBx/mmJSON format | 1dfc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dfc_validation.pdf.gz | 384.5 KB | Display | wwPDB validaton report |
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Full document | 1dfc_full_validation.pdf.gz | 452 KB | Display | |
Data in XML | 1dfc_validation.xml.gz | 27.8 KB | Display | |
Data in CIF | 1dfc_validation.cif.gz | 40.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/df/1dfc ftp://data.pdbj.org/pub/pdb/validation_reports/df/1dfc | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-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: 54601.879 Da / Num. of mol.: 2 / Fragment: FULL-LENGTH PROTEIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: PGEX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: Q16658 |
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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: 2.3 Å3/Da / Density % sol: 46.6 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 4000, hepes, dtt, sodium azide , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 291 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Jun 19, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→23.03 Å / Num. obs: 19147 / % possible obs: 84.2 % / Observed criterion σ(I): 1 / Redundancy: 2.6 % / Biso Wilson estimate: 22.8 Å2 / Rmerge(I) obs: 0.062 / Net I/σ(I): 19.1 |
Reflection | *PLUS Highest resolution: 2.9 Å / Num. obs: 21421 / % possible obs: 94.2 % / Rmerge(I) obs: 0.048 |
-Processing
Software |
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Refinement | Method to determine structure: MIR / Resolution: 2.9→8 Å / σ(F): 0 / Stereochemistry target values: ENGH & HUBER
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Solvent computation | Bsol: 63.17 Å2 / ksol: 0.247 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error free: 0.343 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→8 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 25 Å / Num. reflection obs: 20541 / Rfactor obs: 0.184 / Rfactor Rfree: 0.268 / Rfactor Rwork: 0.223 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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