+Open data
-Basic information
Entry | Database: PDB / ID: 1gc7 | ||||||
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Title | CRYSTAL STRUCTURE OF THE RADIXIN FERM DOMAIN | ||||||
Components | RADIXIN | ||||||
Keywords | CELL ADHESION / 3 subdomains / CYTOSKELETON | ||||||
Function / homology | Function and homology information negative regulation of homotypic cell-cell adhesion / regulation of actin filament bundle assembly / regulation of organelle assembly / regulation of ruffle assembly / establishment of protein localization to plasma membrane / microvillus assembly / negative regulation of adherens junction organization / positive regulation of early endosome to late endosome transport / regulation of Rap protein signal transduction / cell tip ...negative regulation of homotypic cell-cell adhesion / regulation of actin filament bundle assembly / regulation of organelle assembly / regulation of ruffle assembly / establishment of protein localization to plasma membrane / microvillus assembly / negative regulation of adherens junction organization / positive regulation of early endosome to late endosome transport / regulation of Rap protein signal transduction / cell tip / Recycling pathway of L1 / regulation of postsynaptic neurotransmitter receptor diffusion trapping / positive regulation of protein localization to early endosome / stereocilium / apical protein localization / barbed-end actin filament capping / negative regulation of cell size / establishment of endothelial barrier / cellular response to thyroid hormone stimulus / protein kinase A binding / regulation of cell size / cortical actin cytoskeleton / cleavage furrow / microvillus / positive regulation of G1/S transition of mitotic cell cycle / protein kinase A signaling / ruffle / T-tubule / cell adhesion molecule binding / filopodium / cell periphery / protein localization to plasma membrane / adherens junction / establishment of protein localization / positive regulation of protein catabolic process / apical part of cell / lamellipodium / myelin sheath / actin binding / midbody / ATPase binding / regulation of cell shape / positive regulation of cell migration / apical plasma membrane / protein domain specific binding / positive regulation of gene expression / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.8 Å | ||||||
Authors | Hamada, K. / Shimizu, T. / Matsui, T. / Tsukita, S. / Tsukita, S. / Hakoshima, T. | ||||||
Citation | Journal: EMBO J. / Year: 2000 Title: Structural basis of the membrane-targeting and unmasking mechanisms of the radixin FERM domain. Authors: Hamada, K. / Shimizu, T. / Matsui, T. / Tsukita, S. / Hakoshima, T. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2000 Title: Crystallographic characterization of the membrane-binding domain of radixin Authors: Hamada, K. / Shimizu, T. / Matsui, T. / Tsukita, S. / Tsukita, S. / Hakoshima, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gc7.cif.gz | 70.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gc7.ent.gz | 54.2 KB | Display | PDB format |
PDBx/mmJSON format | 1gc7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gc/1gc7 ftp://data.pdbj.org/pub/pdb/validation_reports/gc/1gc7 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 35278.723 Da / Num. of mol.: 1 / Fragment: FERM DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX4T-3 / Production host: Escherichia coli (E. coli) / References: UniProt: P26043 |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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-Sample preparation
Crystal | Density Matthews: 4.37 Å3/Da / Density % sol: 71.87 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 6000, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 4 ℃ | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 288 K |
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Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-6A / Wavelength: 1 |
Detector | Type: ADSC QUAMTUM 4r / Detector: CCD / Date: Mar 2, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. all: 161048 / Num. obs: 23751 / % possible obs: 99.8 % / Biso Wilson estimate: 64.2 Å2 / Rmerge(I) obs: 0.046 / Net I/σ(I): 11.8 |
Reflection shell | Resolution: 2.8→2.9 Å / Rmerge(I) obs: 0.393 / % possible all: 99.9 |
Reflection shell | *PLUS % possible obs: 99.9 % |
-Processing
Software |
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Refinement | Resolution: 2.8→30 Å / σ(F): 2 / Stereochemistry target values: protein.param
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Refinement step | Cycle: LAST / Resolution: 2.8→30 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||
Refine LS restraints | *PLUS
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