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Open data
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Basic information
Entry | Database: PDB / ID: 6len | ||||||
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Title | Structure of NS11 bound FEM1C | ||||||
![]() | Protein fem-1 homolog C,NS11 peptide | ||||||
![]() | PROTEIN BINDING / ubiquitination E3 ligase | ||||||
Function / homology | ![]() ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / negative regulation of non-canonical NF-kappaB signal transduction / Cul2-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / ubiquitin ligase complex / Neddylation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein ubiquitination / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Chen, x. / Liao, S. / Xu, C. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis for arginine C-terminal degron recognition by Cul2 FEM1 E3 ligase. Authors: Chen, X. / Liao, S. / Makaros, Y. / Guo, Q. / Zhu, Z. / Krizelman, R. / Dahan, K. / Tu, X. / Yao, X. / Koren, I. / Xu, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 160.1 KB | Display | ![]() |
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PDB format | ![]() | 122.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 439.4 KB | Display | ![]() |
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Full document | ![]() | 446.4 KB | Display | |
Data in XML | ![]() | 28.6 KB | Display | |
Data in CIF | ![]() | 40.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6lbfSC ![]() 6lbgC ![]() 6lbnC ![]() 6ldpC ![]() 6le6C ![]() 6leyC ![]() 6lf0C ![]() 7cngC 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 45900.355 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: FEM1C fused with NS11 peptide, linked with linker residues GGGSGGGSGGGSGGGS. Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.79 Å3/Da / Density % sol: 67.59 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop Details: 0.2M Sodium citrate tribasic dihydrate, 0.1M Tris pH 8.2 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 7, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→80.652 Å / Num. obs: 54996 / % possible obs: 100 % / Redundancy: 13.1 % / CC1/2: 0.998 / Net I/σ(I): 16.8 |
Reflection shell | Resolution: 2.38→2.51 Å / Num. unique obs: 5405 / CC1/2: 0.823 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6LBF Resolution: 2.383→80.652 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 24.81
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 139.47 Å2 / Biso mean: 63.4071 Å2 / Biso min: 33.89 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.383→80.652 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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