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Open data
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Basic information
Entry | Database: PDB / ID: 4akg | ||||||
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Title | Dynein Motor Domain - ATP complex | ||||||
![]() | GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN HEAVY CHAIN CYTOPLASMIC | ||||||
![]() | MOTOR PROTEIN / AAA+ PROTEIN / ASCE PROTEIN / P-LOOP NTPASE / CYTOSKELETAL MOTOR / ATPASE | ||||||
Function / homology | ![]() karyogamy / establishment of mitotic spindle localization / astral microtubule / nuclear migration along microtubule / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / spindle pole body / cytoplasmic dynein complex / retrograde axonal transport / nuclear migration ...karyogamy / establishment of mitotic spindle localization / astral microtubule / nuclear migration along microtubule / minus-end-directed microtubule motor activity / dynein light intermediate chain binding / spindle pole body / cytoplasmic dynein complex / retrograde axonal transport / nuclear migration / dynein intermediate chain binding / cytoplasmic microtubule / mitotic sister chromatid segregation / establishment of mitotic spindle orientation / glutathione transferase / glutathione transferase activity / cytoplasmic microtubule organization / Neutrophil degranulation / glutathione metabolic process / mitotic spindle organization / cell cortex / ATP hydrolysis activity / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Schmidt, H. / Gleave, E.S. / Carter, A.P. | ||||||
![]() | ![]() Title: Insights Into Dynein Motor Domain Function from a 3.3 Angstrom Crystal Structure Authors: Schmidt, H. / Gleave, E.S. / Carter, A.P. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 849 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 197.2 KB | Display | |
Data in CIF | ![]() | 263 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4ai6SC ![]() 4akhC ![]() 4akiC S: Starting model for refinement C: citing same article ( |
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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: 310205.125 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-218,1364-3038,3292-4092 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() Production host: ![]() ![]() References: UniProt: P08515, UniProt: P36022, glutathione transferase #2: Chemical | #3: Chemical | #4: Chemical | #5: Chemical | ChemComp-SO4 / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.38 Å3/Da / Density % sol: 63.59 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Oct 23, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 3.3→87.7 Å / Num. obs: 113780 / % possible obs: 96.1 % / Observed criterion σ(I): 2 / Redundancy: 5.5 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 3.3→3.56 Å / Redundancy: 5.2 % / Rmerge(I) obs: 1.02 / Mean I/σ(I) obs: 1.7 / % possible all: 86.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4AI6 Resolution: 3.3→50 Å / SU B: 36.109 / SU ML: 0.581 / Cross valid method: THROUGHOUT / σ(F): 2 / ESU R Free: 0.629 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Displacement parameters | Biso mean: 164.076 Å2
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Refinement step | Cycle: LAST / Resolution: 3.3→50 Å
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Refine LS restraints |
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