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Open data
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Basic information
Entry | Database: PDB / ID: 1qpv | ||||||
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Title | YEAST COFILIN | ||||||
![]() | YEAST COFILIN | ||||||
![]() | ACTIN-BINDING PROTEIN / THREE LAYERS:ALPHA/MIXED BETA/ALPHA / COFILIN FOLD | ||||||
Function / homology | ![]() actin filament fragmentation / actin cortical patch / actin filament severing / Golgi to plasma membrane protein transport / actin filament depolymerization / actin filament organization / nuclear matrix / endocytosis / actin filament binding / actin cytoskeleton ...actin filament fragmentation / actin cortical patch / actin filament severing / Golgi to plasma membrane protein transport / actin filament depolymerization / actin filament organization / nuclear matrix / endocytosis / actin filament binding / actin cytoskeleton / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Fedorov, A.A. / Lappalainen, P. / Fedorov, E.V. / Drubin, D.G. / Almo, S.C. | ||||||
![]() | ![]() Title: Structure determination of yeast cofilin. Authors: Fedorov, A.A. / Lappalainen, P. / Fedorov, E.V. / Drubin, D.G. / Almo, S.C. #1: ![]() Title: Essential Functions and Actin-Binding Surfaces of Yeast Cofilin Revealed by Systematic Mutagenesis Authors: Lappalainen, P. / Fedorov, E.V. / Fedorov, A.A. / Almo, S.C. / Drubin, D.G. #2: ![]() Title: Cofilin Promotes Rapid Actin Filament Turnover in Vivo Authors: Lappalainen, P. / Drubin, D.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 36.8 KB | Display | ![]() |
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PDB format | ![]() | 25.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362.2 KB | Display | ![]() |
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Full document | ![]() | 369.4 KB | Display | |
Data in XML | ![]() | 4.6 KB | Display | |
Data in CIF | ![]() | 6.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1cfyC ![]() 1cofSC C: citing same article ( S: Starting model for refinement |
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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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Details | biological unit is monomer |
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Components
#1: Protein | Mass: 15919.742 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.99 Å3/Da / Density % sol: 38 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: PEG 4000 , pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 290 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: Feb 15, 1995 |
Radiation | Monochromator: GRAPHITE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 3→25.2 Å / Num. all: 2529 / Num. obs: 2377 / % possible obs: 89.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 1 / Redundancy: 2.9 % / Biso Wilson estimate: 16.2 Å2 / Rmerge(I) obs: 0.083 / Net I/σ(I): 19.8 |
Reflection shell | Resolution: 3→3.1 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.185 / Mean I/σ(I) obs: 4.9 / % possible all: 77.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1COF Resolution: 3→8 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 2 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 3→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: TOPHCSDX.PRO |