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Open data
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Basic information
Entry | Database: PDB / ID: 3qor | ||||||
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Title | Crystal structure of human nuclear migration protein NudC | ||||||
![]() | (Nuclear migration protein ...) x 4 | ||||||
![]() | PROTEIN BINDING / CELL CYCLE / beta-sandwich / nuclear migration protein / chaperone | ||||||
Function / homology | ![]() nuclear migration / RND2 GTPase cycle / mitotic metaphase chromosome alignment / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / RHO GTPases Activate Formins / mitotic spindle ...nuclear migration / RND2 GTPase cycle / mitotic metaphase chromosome alignment / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / mitotic spindle organization / RHO GTPases Activate Formins / mitotic spindle / response to peptide hormone / spindle / Separation of Sister Chromatids / unfolded protein binding / protein folding / midbody / microtubule / cadherin binding / cell division / nucleoplasm / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Derewenda, U. / Derewenda, Z. / Zheng, M. | ||||||
![]() | ![]() Title: Structural Features and Chaperone Activity of the NudC Protein Family. Authors: Zheng, M. / Cierpicki, T. / Burdette, A.J. / Utepbergenov, D. / Janczyk, P.L. / Derewenda, U. / Stukenberg, P.T. / Caldwell, K.A. / Derewenda, Z.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 146.9 KB | Display | ![]() |
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PDB format | ![]() | 121.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480.7 KB | Display | ![]() |
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Full document | ![]() | 488 KB | Display | |
Data in XML | ![]() | 35 KB | Display | |
Data in CIF | ![]() | 51.8 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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2 | ![]()
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3 | ![]()
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4 | ![]()
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5 | ![]()
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Unit cell |
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Components
-Nuclear migration protein ... , 4 types, 5 molecules ABCDE
#1: Protein | Mass: 13678.567 Da / Num. of mol.: 1 / Fragment: residues 158-274 / Mutation: E236A, K129A Source method: isolated from a genetically manipulated source Details: Cys188 is modified to S-OXY CYSTEINE / Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 13694.566 Da / Num. of mol.: 1 / Fragment: residues 158-274 / Mutation: E236A, K129A Source method: isolated from a genetically manipulated source Details: Cys188 is modified to 3-SULFINOALANINE / Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein | Mass: 13662.567 Da / Num. of mol.: 1 / Fragment: residues 158-274 / Mutation: E236A, K129A Source method: isolated from a genetically manipulated source Details: Cys188 is unmodified / Source: (gene. exp.) ![]() ![]() ![]() |
#4: Protein | Mass: 13710.565 Da / Num. of mol.: 2 / Fragment: residues 158-274 / Mutation: E236A, K129A Source method: isolated from a genetically manipulated source Details: Cys188 is modified to CYSTEINESULFONIC ACID / Source: (gene. exp.) ![]() ![]() ![]() |
-Non-polymers , 2 types, 878 molecules ![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-ACT / |
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#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.55 % |
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 25% PEG 3350, 0.2M sodium acetate, 0.1M lithium sulfate, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: May 5, 2005 |
Radiation | Monochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97928 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→28.05 Å / Num. all: 63806 / Num. obs: 63750 / % possible obs: 99.9 % / Observed criterion σ(F): 1.35 / Observed criterion σ(I): 1 |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.61 Å / VDW probe radii: 0.9 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 49.863 Å2 / ksol: 0.353 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.753→28.05 Å
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Refine LS restraints |
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LS refinement shell |
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