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Open data
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Basic information
Entry | Database: PDB / ID: 1mb8 | ||||||
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Title | Crystal Structure of the actin binding domain of plectin | ||||||
![]() | Plectin![]() | ||||||
![]() | ![]() ![]() ![]() ![]() | ||||||
Function / homology | ![]() protein-containing complex organization / actomyosin contractile ring assembly actin filament organization / skeletal myofibril assembly / tight junction organization / Type I hemidesmosome assembly / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | de Pereda, J.M. | ||||||
![]() | ![]() Title: Structural and Functional Analysis of the Actin Binding Domain of Plectin Suggests Alternative Mechanisms for Binding to F-Actin and Integrin Beta4 Authors: Garcia-Alvarez, B. / Bobkov, A. / Sonnenberg, A. / de Pereda, J.M. | ||||||
History |
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Remark 999 | SEQUENCE AUTHOR INFORMED THAT THE HWRAE INSERTION HAS BEEN DESCRIBED IN MOUSE. AUTHOR ALSO INFORMED ...SEQUENCE AUTHOR INFORMED THAT THE HWRAE INSERTION HAS BEEN DESCRIBED IN MOUSE. AUTHOR ALSO INFORMED THAT RESIDUE ASN 149 IS CORRECT AND THAT THE CONFLICT ON THIS POSITION IS LIKELY DUE TO POLYMORPHISM. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.7 KB | Display | ![]() |
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PDB format | ![]() | 47.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | ![]() Mass: 28444.568 Da / Num. of mol.: 1 / Fragment: Residues 59-293 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.93 Å3/Da / Density % sol: 36.2 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow![]() | *PLUS pH: 7 / Method: vapor diffusion | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 24, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 2.15→35 Å / Num. all: 12571 / Num. obs: 11486 / % possible obs: 91.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Biso Wilson estimate: 12.9 Å2 |
Reflection shell | Resolution: 2.15→2.28 Å / % possible all: 69.2 |
Reflection | *PLUS Lowest resolution: 32 Å / % possible obs: 91.2 % / Num. measured all: 42883 / Rmerge(I) obs: 0.082 |
Reflection shell | *PLUS Lowest resolution: 2.23 Å / % possible obs: 61.4 % / Rmerge(I) obs: 0.319 / Mean I/σ(I) obs: 3.9 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.2332 Å2 / ksol: 0.310086 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.15→31.11 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.28 Å / Rfactor Rfree error: 0.025 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Lowest resolution: 32 Å | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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