+Open data
-Basic information
Entry | Database: PDB / ID: 6le6 | ||||||
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Title | Structure of LNLPTQGRAR bound FEM1C | ||||||
Components | Protein fem-1 homolog C,10-mer peptide | ||||||
Keywords | PROTEIN BINDING / ubiquitination E3 ligase | ||||||
Function / homology | Function and homology information ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / 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 | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.33 Å | ||||||
Authors | Chen, X. / Liao, S. / Xu, C. | ||||||
Funding support | China, 1items
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Citation | Journal: Nat.Chem.Biol. / Year: 2021 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6le6.cif.gz | 301.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6le6.ent.gz | 243.1 KB | Display | PDB format |
PDBx/mmJSON format | 6le6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/le/6le6 ftp://data.pdbj.org/pub/pdb/validation_reports/le/6le6 | HTTPS FTP |
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-Related structure data
Related structure data | 6lbfSC 6lbgC 6lbnC 6ldpC 6lenC 6leyC 6lf0C 7cngC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 45524.996 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: FEM1C fused with a 10-mer peptide LNLPTQGRAR, linked with linker residues GGGSGGGSGGGSGGGS. Source: (gene. exp.) Homo sapiens (human) / Gene: FEM1C, KIAA1785 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96JP0 #2: Chemical | #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.76 Å3/Da / Density % sol: 67.31 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, sitting drop / Details: 0.6M Lithium sulfate, 0.1M BIS-TRIS propane Ph 6.4 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.979 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 17, 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: 2.33→94.52 Å / Num. obs: 57097 / % possible obs: 99.3 % / Redundancy: 13.4 % / CC1/2: 0.999 / Net I/σ(I): 17.9 |
Reflection shell | Resolution: 2.33→2.39 Å / Num. unique obs: 5517 / CC1/2: 0.931 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 6LBF Resolution: 2.33→79.421 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 31.47
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 176.89 Å2 / Biso mean: 71.357 Å2 / Biso min: 33.53 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.33→79.421 Å
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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