+Open data
-Basic information
Entry | Database: PDB / ID: 6d2k | ||||||||||||
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Title | Crystal structure of the FERM domain of mouse FARP2 | ||||||||||||
Components | FERM, ARHGEF and pleckstrin domain-containing protein 2 | ||||||||||||
Keywords | SIGNALING PROTEIN / membrane targeting | ||||||||||||
Function / homology | Function and homology information regulation of integrin activation / hair cycle process / RAC1 GTPase cycle / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / podosome assembly / neuron remodeling / Rac protein signal transduction / semaphorin-plexin signaling pathway / cytoskeletal protein binding / guanyl-nucleotide exchange factor activity ...regulation of integrin activation / hair cycle process / RAC1 GTPase cycle / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / podosome assembly / neuron remodeling / Rac protein signal transduction / semaphorin-plexin signaling pathway / cytoskeletal protein binding / guanyl-nucleotide exchange factor activity / osteoclast differentiation / actin cytoskeleton organization / cytoskeleton / cell adhesion / cytosol / cytoplasm Similarity search - Function | ||||||||||||
Biological species | Mus musculus (house mouse) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||||||||
Authors | He, X. / Zhang, X. | ||||||||||||
Funding support | United States, China, 3items
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Citation | Journal: Sci Rep / Year: 2018 Title: Structural analyses of FERM domain-mediated membrane localization of FARP1. Authors: Kuo, Y.C. / He, X. / Coleman, A.J. / Chen, Y.J. / Dasari, P. / Liou, J. / Biederer, T. / Zhang, X. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6d2k.cif.gz | 80.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6d2k.ent.gz | 57.4 KB | Display | PDB format |
PDBx/mmJSON format | 6d2k.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d2/6d2k ftp://data.pdbj.org/pub/pdb/validation_reports/d2/6d2k | HTTPS FTP |
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-Related structure data
Related structure data | 6d21C 6d2qC 2he7S C: citing same article (ref.) S: Starting model for refinement |
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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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-Components
#1: Protein | Mass: 34198.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Farp2, Kiaa0793 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q91VS8 |
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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: 1.98 Å3/Da / Density % sol: 37.74 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 0.1 M Sodium acetate trihydrate, 12 % PEG 3350 (w/v) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97935 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 19, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97935 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→36.38 Å / Num. obs: 37895 / % possible obs: 99.7 % / Redundancy: 5.4 % / Net I/σ(I): 34.02 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2HE7 Resolution: 1.55→36.38 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 0.12 / Phase error: 22.13
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Bsol: 60.297 Å2 / ksol: 0.4 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.55→36.38 Å
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Refine LS restraints |
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LS refinement shell |
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