+
Open data
-
Basic information
Entry | Database: PDB / ID: 2kin | ||||||
---|---|---|---|---|---|---|---|
Title | KINESIN (MONOMERIC) FROM RATTUS NORVEGICUS | ||||||
![]() | (KINESIN) x 2 | ||||||
![]() | MOTOR PROTEIN / CYTOSKELETON | ||||||
Function / homology | ![]() response to rotenone / RHO GTPases activate KTN1 / Kinesins / distal axon / anterograde dendritic transport of messenger ribonucleoprotein complex / COPI-dependent Golgi-to-ER retrograde traffic / anterograde dendritic transport of neurotransmitter receptor complex / central region of growth cone / anterograde axonal protein transport / MHC class II antigen presentation ...response to rotenone / RHO GTPases activate KTN1 / Kinesins / distal axon / anterograde dendritic transport of messenger ribonucleoprotein complex / COPI-dependent Golgi-to-ER retrograde traffic / anterograde dendritic transport of neurotransmitter receptor complex / central region of growth cone / anterograde axonal protein transport / MHC class II antigen presentation / retrograde neuronal dense core vesicle transport / apolipoprotein receptor binding / intracellular mRNA localization / thalamus development / apical dendrite / cellular response to ethanol / plus-end-directed microtubule motor activity / motor neuron axon guidance / postsynaptic cytosol / ciliary rootlet / microtubule motor activity / kinesin complex / synaptic vesicle transport / kinesin binding / microtubule-based process / neuron development / mRNA transport / axonal growth cone / vesicle-mediated transport / axon cytoplasm / dendrite cytoplasm / cellular response to nerve growth factor stimulus / hippocampus development / axon guidance / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / P-body / cerebral cortex development / mitotic cell cycle / scaffold protein binding / microtubule binding / perikaryon / microtubule / neuron projection / axon / neuronal cell body / dendrite / protein-containing complex binding / perinuclear region of cytoplasm / ATP hydrolysis activity / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sack, S. / Muller, J. / Kozielski, F. / Marx, A. / Thormahlen, M. / Biou, V. / Mandelkow, E.-M. / Brady, S.T. / Mandelkow, E. | ||||||
![]() | ![]() Title: X-ray structure of motor and neck domains from rat brain kinesin. Authors: Sack, S. / Muller, J. / Marx, A. / Thormahlen, M. / Mandelkow, E.M. / Brady, S.T. / Mandelkow, E. #1: ![]() Title: Crystallization and Preliminary X-Ray Analysis of the Single-Headed and Double-Headed Motor Protein Kinesin Authors: Kozielski, F. / Schonbrunn, E. / Sack, S. / Muller, J. / Brady, S.T. / Mandelkow, E. #2: ![]() Title: The Crystal Structure of Dimeric Kinesin and Implications for Microtubule-Dependent Motility Authors: Kozielski, F. / Sack, S. / Marx, A. / Thormahlen, M. / Schonbrunn, E. / Biou, V. / Thompson, A. / Mandelkow, E.M. / Mandelkow, E. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 85.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 63.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 469.4 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 480 KB | Display | |
Data in XML | ![]() | 10.2 KB | Display | |
Data in CIF | ![]() | 15.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 27072.869 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN, MOTOR DOMAIN / Mutation: G293D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
---|---|---|---|---|---|
#2: Protein | Mass: 11169.800 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN, MOTOR DOMAIN / Mutation: G293D Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
#3: Chemical | #4: Chemical | ChemComp-ADP / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.6 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Method: vapor diffusion, hanging drop / pH: 7.5 Details: HANGING DROP METHOD WAS USED. PROTEIN WAS CRYSTALLIZED FROM 20MM PIPES, PH 7.5, 50MM KCL, 1MM EGTA, 1MM DTT, 0.9 M LI2SO4. THE RESERVOIR CONTAINED 1.8 M LITHIUM SULFATE IN THE SAME BUFFER., ...Details: HANGING DROP METHOD WAS USED. PROTEIN WAS CRYSTALLIZED FROM 20MM PIPES, PH 7.5, 50MM KCL, 1MM EGTA, 1MM DTT, 0.9 M LI2SO4. THE RESERVOIR CONTAINED 1.8 M LITHIUM SULFATE IN THE SAME BUFFER., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 90 K |
---|---|
Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 28, 1996 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 32107 / % possible obs: 99.3 % / Redundancy: 5.1 % / Rsym value: 0.048 / Net I/σ(I): 13.6 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 4.2 % / Rsym value: 0.19 / % possible all: 98.8 |
Reflection | *PLUS Num. measured all: 301422 / Rmerge(I) obs: 0.048 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: UNREFINED KINESIN DIMER Resolution: 2→6 Å / Cross valid method: FREE R
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→6 Å
| ||||||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.194 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 24.3 Å2 | ||||||||||||||||||||
Refine LS restraints | *PLUS
|