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Open data
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Basic information
Entry | Database: PDB / ID: 3ue5 | ||||||
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Title | ECP-cleaved Actin in complex with Spir domain D | ||||||
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![]() | CONTRACTILE PROTEIN/TRANSPORT PROTEIN / CONTRACTILE PROTEIN / CONTRACTILE PROTEIN-TRANSPORT PROTEIN complex | ||||||
Function / homology | ![]() chorion-containing eggshell formation / pole plasm RNA localization / oocyte karyosome formation / establishment of meiotic spindle localization / actin filament-based process / pole plasm oskar mRNA localization / pole plasm assembly / polar body extrusion after meiotic divisions / actin filament network formation / actin nucleation ...chorion-containing eggshell formation / pole plasm RNA localization / oocyte karyosome formation / establishment of meiotic spindle localization / actin filament-based process / pole plasm oskar mRNA localization / pole plasm assembly / polar body extrusion after meiotic divisions / actin filament network formation / actin nucleation / Golgi vesicle transport / cleavage furrow formation / cytoskeletal motor activator activity / oogenesis / tropomyosin binding / mesenchyme migration / troponin I binding / regulation of cytoskeleton organization / myosin heavy chain binding / filamentous actin / actin filament bundle / skeletal muscle thin filament assembly / striated muscle thin filament / actin filament bundle assembly / skeletal muscle myofibril / actin monomer binding / intracellular transport / skeletal muscle fiber development / stress fiber / titin binding / vesicle-mediated transport / actin filament polymerization / filopodium / actin filament organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cytoplasmic vesicle membrane / calcium-dependent protein binding / protein transport / lamellipodium / actin binding / cell cortex / cell body / actin cytoskeleton organization / microtubule binding / cytoskeleton / hydrolase activity / protein domain specific binding / calcium ion binding / positive regulation of gene expression / perinuclear region of cytoplasm / magnesium ion binding / ATP binding / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() ![]() | ||||||
![]() | Chen, C. / Phillips, M. / Sawaya, M.R. / Ralston, C.Y. / Quinlan, M.E. | ||||||
![]() | ![]() Title: Multiple Forms of Spire-Actin Complexes and their Functional Consequences. Authors: Chen, C.K. / Sawaya, M.R. / Phillips, M.L. / Reisler, E. / Quinlan, M.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 165.9 KB | Display | ![]() |
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PDB format | ![]() | 135.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 41862.613 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: skeletal / Source: (natural) ![]() ![]() |
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#2: Protein | Mass: 7320.585 Da / Num. of mol.: 1 / Fragment: UNP residues 428-485 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 44 molecules ![](data/chem/img/CA.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ATP.gif)
![](data/chem/img/CL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CA / | ||
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#4: Chemical | ChemComp-ATP / | ||
#5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.99 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: Tris pH 8.5, magnesium chloride, PEG-8000, vapor diffusion, hanging drop, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 5, 2008 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.76→90 Å / Num. all: 10542 / Num. obs: 10542 / % possible obs: 89.6 % / Observed criterion σ(I): -3 / Redundancy: 2.7 % / Biso Wilson estimate: 46 Å2 / Rmerge(I) obs: 0.105 / Χ2: 0.963 / Net I/σ(I): 8.8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Phasing
Phasing | Method: ![]() | |||||||||
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Phasing MR | Model details: Phaser MODE: MR_AUTO
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso max: 149.31 Å2 / Biso mean: 48.4404 Å2 / Biso min: 15.64 Å2
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Refine analyze | Luzzati coordinate error obs: 0.364 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.76→50.24 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.76→3.08 Å / Total num. of bins used: 5
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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