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Open data
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Basic information
| Entry | Database: PDB / ID: 9nfq | ||||||
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| Title | Crystal structure of CRBN-DDB1 and MRT-3486 in complex with NEK7 | ||||||
Components |
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Keywords | DNA Binding Protein/Transferase / Ternary complex / Molecular glue degrader / neosubstrate / DNA Binding Protein-Transferase complex | ||||||
| Function / homology | Function and homology informationNEK6-subfamily protein kinase / Activation of NIMA Kinases NEK9, NEK6, NEK7 / negative regulation of monoatomic ion transmembrane transport / Nuclear Pore Complex (NPC) Disassembly / positive regulation by virus of viral protein levels in host cell / spindle assembly involved in female meiosis / cellular response to potassium ion / epigenetic programming in the zygotic pronuclei / UV-damage excision repair / biological process involved in interaction with symbiont ...NEK6-subfamily protein kinase / Activation of NIMA Kinases NEK9, NEK6, NEK7 / negative regulation of monoatomic ion transmembrane transport / Nuclear Pore Complex (NPC) Disassembly / positive regulation by virus of viral protein levels in host cell / spindle assembly involved in female meiosis / cellular response to potassium ion / epigenetic programming in the zygotic pronuclei / UV-damage excision repair / biological process involved in interaction with symbiont / regulation of mitotic cell cycle phase transition / WD40-repeat domain binding / Cul4A-RING E3 ubiquitin ligase complex / Cul4-RING E3 ubiquitin ligase complex / Cul4B-RING E3 ubiquitin ligase complex / positive regulation of NLRP3 inflammasome complex assembly / ubiquitin ligase complex scaffold activity / negative regulation of reproductive process / negative regulation of developmental process / positive regulation of telomere maintenance / microtubule organizing center / locomotory exploration behavior / viral release from host cell / cullin family protein binding / positive regulation of Wnt signaling pathway / ectopic germ cell programmed cell death / negative regulation of protein-containing complex assembly / positive regulation of viral genome replication / proteasomal protein catabolic process / spindle assembly / positive regulation of gluconeogenesis / EML4 and NUDC in mitotic spindle formation / regulation of mitotic cell cycle / molecular function activator activity / nucleotide-excision repair / positive regulation of protein-containing complex assembly / Recognition of DNA damage by PCNA-containing replication complex / regulation of circadian rhythm / DNA Damage Recognition in GG-NER / 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 / spindle pole / 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 / site of double-strand break / Neddylation / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / Potential therapeutics for SARS / proteasome-mediated ubiquitin-dependent protein catabolic process / microtubule / damaged DNA binding / transmembrane transporter binding / chromosome, telomeric region / protein phosphorylation / protein ubiquitination / protein serine kinase activity / DNA repair / protein serine/threonine kinase activity / apoptotic process / DNA damage response / centrosome / negative regulation of apoptotic process / protein-containing complex binding / nucleolus / perinuclear region of cytoplasm / protein-containing complex / extracellular space / DNA binding / extracellular exosome / nucleoplasm / ATP binding / metal ion binding / nucleus / membrane / cytosol / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å | ||||||
Authors | Quan, C. / Petzold, G. / Bunker, R.D. / Wiedmer, L. / Gainza, P. / Tsai, J.H.C. | ||||||
| Funding support | 1items
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Citation | Journal: Science / Year: 2025Title: Mining the CRBN target space redefines rules for molecular glue-induced neosubstrate recognition. Authors: Petzold, G. / Gainza, P. / Annunziato, S. / Lamberto, I. / Trenh, P. / McAllister, L.A. / DeMarco, B. / Schwander, L. / Bunker, R.D. / Zlotosch, M. / SriRamaratnam, R. / Gilberto, S. / ...Authors: Petzold, G. / Gainza, P. / Annunziato, S. / Lamberto, I. / Trenh, P. / McAllister, L.A. / DeMarco, B. / Schwander, L. / Bunker, R.D. / Zlotosch, M. / SriRamaratnam, R. / Gilberto, S. / Langousis, G. / Donckele, E.J. / Quan, C. / Strande, V. / De Donatis, G.M. / Alabi, S.B. / Alers, J. / Matysik, M. / Staehly, C. / Dubois, A. / Osmont, A. / Garskovas, M. / Lyon, D. / Wiedmer, L. / Oleinikovas, V. / Lieberherr, R. / Rubin, N.T. / Lam, D.T. / Lucas, X. / Liardo, E. / Widlund, N.I. / Ritzen, A. / Caceres, R.M. / Vigil, D. / Tsai, J. / Wallace, O. / Peluso, M. / Sadok, A. / Tiedt, R. / Paterson, A.M. / Zarayskiy, V. / Fasching, B. / Bonenfant, D. / Warmuth, M. / Castle, J.C. / Townson, S.A. | ||||||
| History |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 9nfq.cif.gz | 694.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9nfq.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9nfq.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9nfq_validation.pdf.gz | 999.6 KB | Display | wwPDB validaton report |
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| Full document | 9nfq_full_validation.pdf.gz | 1002 KB | Display | |
| Data in XML | 9nfq_validation.xml.gz | 53.1 KB | Display | |
| Data in CIF | 9nfq_validation.cif.gz | 71.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nf/9nfq ftp://data.pdbj.org/pub/pdb/validation_reports/nf/9nfq | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9nfrC ![]() 9ngtC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| Unit cell |
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Components
-Protein , 3 types, 3 molecules ABC
| #1: Protein | Mass: 127097.469 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: DDB1, XAP1 / Production host: ![]() |
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| #2: Protein | Mass: 50603.676 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CRBN, AD-006 / Production host: ![]() |
| #3: Protein | Mass: 34841.242 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: NEK7 / Production host: ![]() |
-Non-polymers , 4 types, 4 molecules 




| #4: Chemical | ChemComp-A1BX6 / ( Mass: 572.635 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H28N6O5S / Feature type: SUBJECT OF INVESTIGATION |
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| #5: Chemical | ChemComp-ZN / |
| #6: Chemical | ChemComp-ADP / |
| #7: Chemical | ChemComp-MG / |
-Details
| Has ligand of interest | Y |
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| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.029 M HEPES salt, 0.071 M MOPS acid, 0.06 M NaNO3, 0.06 M Na2HPO4, 0.06 M (NH4)2SO4, 11 % (w/v) PEG 8,000 and 25 % (v/v) ethylene glycol. |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X13 / Wavelength: 0.95372 Å |
| Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 6, 2023 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.95372 Å / Relative weight: 1 |
| Reflection | Resolution: 3.25→46.61 Å / Num. obs: 24342 / % possible obs: 94.3 % / Redundancy: 13.1 % / CC1/2: 0.995 / Rmerge(I) obs: 0.236 / Net I/σ(I): 7.3 |
| Reflection shell | Resolution: 3.25→3.4 Å / Num. unique obs: 1478 / CC1/2: 0.612 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.25→46.61 Å / SU ML: 0.4214 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 27.0093 Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 95.44 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.25→46.61 Å
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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| Refinement TLS group | Refine-ID: X-RAY DIFFRACTION
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Homo sapiens (human)
X-RAY DIFFRACTION
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