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- PDB-1vom: COMPLEX BETWEEN DICTYOSTELIUM MYOSIN AND MGADP AND VANADATE AT 1.... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1vom | ||||||
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Title | COMPLEX BETWEEN DICTYOSTELIUM MYOSIN AND MGADP AND VANADATE AT 1.9A RESOLUTION | ||||||
![]() | MYOSIN | ||||||
![]() | MUSCLE PROTEIN / MYOSIN / MOLECULAR MOTOR / TRANSITION-STATE ANALOG | ||||||
Function / homology | ![]() calcium-dependent ATPase activity / pseudopodium retraction / uropod retraction / cytoplasmic actin-based contraction involved in forward cell motility / phagocytic cup base / pathogen-containing vacuole / equatorial cell cortex / contractile actin filament bundle assembly / cell trailing edge / contractile vacuole organization ...calcium-dependent ATPase activity / pseudopodium retraction / uropod retraction / cytoplasmic actin-based contraction involved in forward cell motility / phagocytic cup base / pathogen-containing vacuole / equatorial cell cortex / contractile actin filament bundle assembly / cell trailing edge / contractile vacuole organization / myosin filament assembly / aggregation involved in sorocarp development / culmination involved in sorocarp development / RHO GTPases activate PAKs / adenyl nucleotide binding / response to differentiation-inducing factor 1 / hypotonic response / uropod / mitotic actomyosin contractile ring / actomyosin contractile ring / mitotic actomyosin contractile ring contraction / actin-myosin filament sliding / detection of mechanical stimulus / apical cortex / negative regulation of actin filament polymerization / bleb assembly / actomyosin / substrate-dependent cell migration, cell extension / myosin filament / filopodium assembly / early phagosome / cortical actin cytoskeleton organization / myosin II complex / cortical actin cytoskeleton / microfilament motor activity / pseudopodium / cytoskeletal motor activity / cleavage furrow / mitotic cytokinesis / response to mechanical stimulus / 14-3-3 protein binding / response to cAMP / extracellular matrix / muscle contraction / cell motility / response to hydrogen peroxide / protein localization / chemotaxis / actin filament binding / cell cortex / regulation of cell shape / cytoplasmic vesicle / cytoskeleton / calmodulin binding / ATP binding / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Rayment, I. / Smith, C.A. | ||||||
![]() | ![]() Title: X-ray structure of the magnesium(II).ADP.vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Authors: Smith, C.A. / Rayment, I. #1: ![]() Title: Structural Studies of Myosin:Nucleotide Complexes: A Revised Model for the Molecular Basis of Muscle Contraction Authors: Fisher, A.J. / Smith, C.A. / Thoden, J. / Smith, R. / Sutoh, K. / Holden, H.M. / Rayment, I. #2: ![]() Title: X-Ray Structures of the Myosin Motor Domain of Dictyostelium Discoideum Complexed with Mgadp.Befx and Mgadp.Alf4- Authors: Fisher, A.J. / Smith, C.A. / Thoden, J.B. / Smith, R. / Sutoh, K. / Holden, H.M. / Rayment, I. #3: ![]() Title: Three-Dimensional Structure of Myosin Subfragment-1: A Molecular Motor Authors: Rayment, I. / Rypniewski, W.R. / Schmidt-Base, K. / Smith, R. / Tomchick, D.R. / Benning, M.M. / Winkelmann, D.A. / Wesenberg, G. / Holden, H.M. #4: ![]() Title: Force-Generating Domain of Myosin Motor Authors: Itakura, S. / Yamakawa, H. / Toyoshima, Y.Y. / Ishijima, A. / Kojima, T. / Harada, Y. / Yanagida, T. / Wakabayashi, T. / Sutoh, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 178.1 KB | Display | ![]() |
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PDB format | ![]() | 136.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 463.2 KB | Display | ![]() |
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Full document | ![]() | 491.7 KB | Display | |
Data in XML | ![]() | 19.1 KB | Display | |
Data in CIF | ![]() | 32.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 86749.008 Da / Num. of mol.: 1 / Fragment: TRUNCATED AT RESIDUE 762 Source method: isolated from a genetically manipulated source Details: THIS MOLECULE WAS TRUNCATED TO YIELD A FRAGMENT THAT CRYSTALLIZES READILY Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-VO4 / |
#4: Chemical | ChemComp-ADP / |
#5: Water | ChemComp-HOH / |
Compound details | SSBOND THIS LIES BETWEEN TWOFOLD RELATED MOLECULES. |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.45 Å3/Da / Density % sol: 77.41 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7 / Method: batch method | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.08 |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE AREA DETECTOR / Date: Feb 1, 1995 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.08 Å / Relative weight: 1 |
Reflection | Num. obs: 75066 / % possible obs: 97 % / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.028 |
Reflection | *PLUS Highest resolution: 1.9 Å / Num. measured all: 393986 |
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Processing
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Refinement | Resolution: 1.9→30 Å / σ(F): 0 /
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Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 20 Å / Rfactor all: 0.194 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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