+Open data
-Basic information
Entry | Database: PDB / ID: 3kin | ||||||
---|---|---|---|---|---|---|---|
Title | KINESIN (DIMERIC) FROM RATTUS NORVEGICUS | ||||||
Components | (KINESIN HEAVY CHAIN) x 2 | ||||||
Keywords | MOTOR PROTEIN / CYTOSKELETON | ||||||
Function / homology | Function and homology information 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 / thalamus development / intracellular mRNA localization / apical dendrite / cellular response to ethanol / motor neuron axon guidance / plus-end-directed microtubule motor activity / microtubule motor activity / ciliary rootlet / kinesin complex / synaptic vesicle transport / postsynaptic cytosol / kinesin binding / microtubule-based process / GABA-ergic synapse / mRNA transport / neuron development / axonal growth cone / vesicle-mediated transport / axon cytoplasm / dendrite cytoplasm / cellular response to nerve growth factor stimulus / axon guidance / hippocampus development / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / P-body / cerebral cortex development / 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 | Rattus norvegicus (Norway rat) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MIRAS / Resolution: 3.1 Å | ||||||
Authors | Kozielski, F. / Sack, S. / Marx, A. / Thormahlen, M. / Schonbrunn, E. / Biou, V. / Thompson, A. / Mandelkow, E.-M. / Mandelkow, E. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1997 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. #1: Journal: J.Struct.Biol. / Year: 1997 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: Journal: Biochemistry / Year: 1997 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. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 3kin.cif.gz | 132.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb3kin.ent.gz | 107.6 KB | Display | PDB format |
PDBx/mmJSON format | 3kin.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3kin_validation.pdf.gz | 531.6 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 3kin_full_validation.pdf.gz | 616.4 KB | Display | |
Data in XML | 3kin_validation.xml.gz | 29.2 KB | Display | |
Data in CIF | 3kin_validation.cif.gz | 40.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ki/3kin ftp://data.pdbj.org/pub/pdb/validation_reports/ki/3kin | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 27072.869 Da / Num. of mol.: 2 / Fragment: MOTOR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Production host: Escherichia coli (E. coli) / References: UniProt: P56536*PLUS #2: Protein | Mass: 13248.242 Da / Num. of mol.: 2 / Fragment: MOTOR DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) Rattus norvegicus (Norway rat) / Organ: BRAIN / Production host: Escherichia coli (E. coli) / References: UniProt: Q6QLM7*PLUS #3: Chemical | #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 55 % | ||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
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, 200MM NACL, 2MM DTT, 2 MM NA-EGTA, 0.8 M AS. THE RESERVOIR CONTAINED 1.6 M AS IN THE SAME BUFFER., vapor diffusion - hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||
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: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jul 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. obs: 19516 / % possible obs: 100 % / Rsym value: 0.064 / Net I/σ(I): 10.7 |
Reflection | *PLUS Num. measured all: 113071 / Rmerge(I) obs: 0.064 |
-Processing
Software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MIRAS / Resolution: 3.1→6 Å / Cross valid method: FREE R
| |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.1→6 Å
|