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- PDB-6uml: Structural Basis for Thalidomide Teratogenicity Revealed by the C... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6uml | ||||||
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Title | Structural Basis for Thalidomide Teratogenicity Revealed by the Cereblon-DDB1-SALL4-Pomalidomide Complex | ||||||
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![]() | LIGASE / CELMoD / cereblon-CRL4 / ubiquitin ligase / C2H2 zinc finger | ||||||
Function / homology | ![]() POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / negative regulation of monoatomic ion transmembrane transport / Transcriptional regulation of pluripotent stem cells / 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 / embryonic limb morphogenesis / biological process involved in interaction with symbiont ...POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / negative regulation of monoatomic ion transmembrane transport / Transcriptional regulation of pluripotent stem cells / 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 / embryonic limb morphogenesis / biological process involved in interaction with symbiont / WD40-repeat domain binding / ventricular septum development / regulation of mitotic cell cycle phase transition / Cul4A-RING E3 ubiquitin ligase complex / inner cell mass cell proliferation / Cul4B-RING E3 ubiquitin ligase complex / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / locomotory exploration behavior / somatic stem cell population maintenance / cullin family protein binding / viral release from host cell / positive regulation of Wnt signaling pathway / ectopic germ cell programmed cell death / proteasomal protein catabolic process / positive regulation of viral genome replication / negative regulation of protein-containing complex assembly / heterochromatin / positive regulation of gluconeogenesis / Regulation of PTEN gene transcription / neural tube closure / nucleotide-excision repair / Recognition of DNA damage by PCNA-containing replication complex / DNA Damage Recognition in GG-NER / positive regulation of protein-containing complex assembly / regulation of circadian rhythm / Dual Incision in GG-NER / 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 / Neddylation / site of double-strand break / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / transmembrane transporter binding / Potential therapeutics for SARS / chromosome, telomeric region / damaged DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / protein ubiquitination / RNA polymerase II cis-regulatory region sequence-specific DNA binding / intracellular membrane-bounded organelle / DNA repair / apoptotic process / DNA damage response / protein-containing complex binding / nucleolus / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / perinuclear region of cytoplasm / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular space / extracellular exosome / nucleoplasm / membrane / nucleus / metal ion binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Clayton, T.L. / Matyskiela, M.E. / Pagarigan, B.E. / Tran, E.T. / Chamberlain, P.P. | ||||||
![]() | ![]() Title: Crystal structure of the SALL4-pomalidomide-cereblon-DDB1 complex. Authors: Matyskiela, M.E. / Clayton, T. / Zheng, X. / Mayne, C. / Tran, E. / Carpenter, A. / Pagarigan, B. / McDonald, J. / Rolfe, M. / Hamann, L.G. / Lu, G. / Chamberlain, P.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 658 KB | Display | ![]() |
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PDB format | ![]() | 451 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 329.1 KB | Display | ![]() |
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Full document | ![]() | 330 KB | Display | |
Data in XML | ![]() | 1.6 KB | Display | |
Data in CIF | ![]() | 15 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4tz4S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 127097.469 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein | Mass: 46596.566 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
#3: Protein/peptide | Mass: 3260.777 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
#4: Chemical | #5: Chemical | ChemComp-Y70 / | Has ligand of interest | Y | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.9 Å3/Da / Density % sol: 57.56 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 10% PEG MME 500, 8% PEG 20K, 210mM calcium acetate, 100mM tris pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Feb 6, 2019 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97931 Å / Relative weight: 1 |
Reflection | Resolution: 3.58→38.7 Å / Num. obs: 23629 / % possible obs: 98.42 % / Redundancy: 3.4 % / Biso Wilson estimate: 79.26 Å2 / CC1/2: 0.964 / Rmerge(I) obs: 0.1637 / Rpim(I) all: 0.1042 / Rrim(I) all: 0.1948 / Net I/σ(I): 5.04 |
Reflection shell | Resolution: 3.58→3.64 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.5699 / Num. unique obs: 2336 / CC1/2: 0.734 / Rpim(I) all: 0.3551 / Rrim(I) all: 0.6734 / % possible all: 98.11 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4TZ4 Resolution: 3.58→38.7 Å / SU ML: 0.5122 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.413 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 85.16 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.58→38.7 Å
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Refine LS restraints |
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LS refinement shell |
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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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