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Yorodumi- PDB-4ci1: Structure of the DDB1-CRBN E3 ubiquitin ligase bound to thalidomide -
+Open data
-Basic information
Entry | Database: PDB / ID: 4ci1 | ||||||
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Title | Structure of the DDB1-CRBN E3 ubiquitin ligase bound to thalidomide | ||||||
Components |
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Keywords | DNA BINDING PROTEIN/PROTEIN / DNA BINDING PROTEIN-PROTEIN COMPLEX / DNA BINDING PROTEIN-PROTEIN BINDING COMPLEX / UBIQUITIN / CONT | ||||||
Function / homology | Function and homology information positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / Cul4A-RING E3 ubiquitin ligase complex / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4B-RING E3 ubiquitin ligase complex ...positive regulation by virus of viral protein levels in host cell / epigenetic programming in the zygotic pronuclei / spindle assembly involved in female meiosis / Cul4-RING E3 ubiquitin ligase complex / UV-damage excision repair / biological process involved in interaction with symbiont / Cul4A-RING E3 ubiquitin ligase complex / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / cullin family protein binding / viral release from host cell / ectopic germ cell programmed cell death / positive regulation of viral genome replication / positive regulation of gluconeogenesis / proteasomal protein catabolic process / Recognition of DNA damage by PCNA-containing replication complex / nucleotide-excision repair / DNA Damage Recognition in GG-NER / Dual Incision in GG-NER / regulation of circadian rhythm / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / Wnt signaling pathway / Formation of Incision Complex in GG-NER / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / positive regulation of protein catabolic process / cellular response to UV / rhythmic process / protein-macromolecule adaptor activity / site of double-strand break / Neddylation / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / chromosome, telomeric region / damaged DNA binding / protein ubiquitination / DNA repair / apoptotic process / DNA damage response / protein-containing complex binding / nucleolus / negative regulation of apoptotic process / protein-containing complex / DNA binding / extracellular space / extracellular exosome / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) GALLUS GALLUS (chicken) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.98 Å | ||||||
Authors | Fischer, E.S. / Boehm, K. / Thoma, N.H. | ||||||
Citation | Journal: Nature / Year: 2014 Title: Structure of the Ddb1-Crbn E3 Ubiquitin Ligase in Complex with Thalidomide. Authors: Fischer, E.S. / Bohm, K. / Lydeard, J.R. / Yang, H. / Stadler, M.B. / Cavadini, S. / Nagel, J. / Serluca, F. / Acker, V. / Lingaraju, G.M. / Tichkule, R.B. / Schebesta, M. / Forrester, W.C. ...Authors: Fischer, E.S. / Bohm, K. / Lydeard, J.R. / Yang, H. / Stadler, M.B. / Cavadini, S. / Nagel, J. / Serluca, F. / Acker, V. / Lingaraju, G.M. / Tichkule, R.B. / Schebesta, M. / Forrester, W.C. / Schirle, M. / Hassiepen, U. / Ottl, J. / Hild, M. / Beckwith, R.E.J. / Harper, J.W. / Jenkins, J.L. / Thoma, N.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4ci1.cif.gz | 589 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4ci1.ent.gz | 497.6 KB | Display | PDB format |
PDBx/mmJSON format | 4ci1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ci/4ci1 ftp://data.pdbj.org/pub/pdb/validation_reports/ci/4ci1 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 129493.852 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PFASTBAC DUAL / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: Q16531 |
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#2: Protein | Mass: 54207.148 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) GALLUS GALLUS (chicken) / Plasmid: PFASTBAC DUAL / Cell line (production host): High Five / Production host: TRICHOPLUSIA NI (cabbage looper) / References: UniProt: P0CF65 |
#3: Chemical | ChemComp-ZN / |
#4: Chemical | ChemComp-EF2 / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.18 Å3/Da / Density % sol: 64 % / Description: NONE |
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Crystal grow | pH: 6 Details: PROTEIN WAS CRYSTALLIZED FROM 100 MM NA-CACODYLATE; 80 MM NAH2PO4; 120 MM K2HPO4; 800 MM TRI-NA CITRATE., pH 6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99999 |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 22, 2012 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99999 Å / Relative weight: 1 |
Reflection | Resolution: 2.98→30 Å / Num. obs: 49202 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 7.9 % / Biso Wilson estimate: 97.97 Å2 / Rmerge(I) obs: 0.12 / Net I/σ(I): 15.77 |
Reflection shell | Resolution: 2.98→3.06 Å / Redundancy: 5.6 % / Rmerge(I) obs: 1.37 / Mean I/σ(I) obs: 1.22 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: DDB1 Resolution: 2.98→29.82 Å / Cor.coef. Fo:Fc: 0.9359 / Cor.coef. Fo:Fc free: 0.9044 / SU R Cruickshank DPI: 1.08 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.89 / SU Rfree Blow DPI: 0.324 / SU Rfree Cruickshank DPI: 0.334
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Displacement parameters | Biso mean: 87.64 Å2
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Refine analyze | Luzzati coordinate error obs: 0.483 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.98→29.82 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.98→3.06 Å / Total num. of bins used: 20
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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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