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Yorodumi- PDB-1nj3: Structure and Ubiquitin Interactions of the Conserved NZF Domain ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1nj3 | ||||||
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| Title | Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4 | ||||||
Components | NPL4 | ||||||
Keywords | PROTEIN BINDING / NZF domain / Npl4 / rubredoxin knuckle / beta-ribbon / zinc-finger / ubiquitin | ||||||
| Function / homology | Function and homology informationTranslesion Synthesis by POLH / UFD1-NPL4 complex / Neddylation / negative regulation of RIG-I signaling pathway / KEAP1-NFE2L2 pathway / VCP-NPL4-UFD1 AAA ATPase complex / negative regulation of type I interferon production / retrograde protein transport, ER to cytosol / Golgi organization / ERAD pathway ...Translesion Synthesis by POLH / UFD1-NPL4 complex / Neddylation / negative regulation of RIG-I signaling pathway / KEAP1-NFE2L2 pathway / VCP-NPL4-UFD1 AAA ATPase complex / negative regulation of type I interferon production / retrograde protein transport, ER to cytosol / Golgi organization / ERAD pathway / ubiquitin binding / ATPase binding / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / ubiquitin protein ligase binding / protein-containing complex binding / zinc ion binding / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / Torsion Angle Dynamics, Simulated annealing | ||||||
Authors | Wang, B. / Alam, S.L. / Meyer, H.H. / Payne, M. / Stemmler, T.L. / Davis, D.R. / Sundquist, W.I. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2003Title: Structure and ubiquitin interactions of the conserved zinc finger domain of Npl4. Authors: Wang, B. / Alam, S.L. / Meyer, H.H. / Payne, M. / Stemmler, T.L. / Davis, D.R. / Sundquist, W.I. #1: Journal: Embo J. / Year: 2000Title: A complex of mammalian ufd1 and nlp4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport Authors: Meyer, H.H. / Shorter, J.G. / Pappin, D. / Warren, G. #2: Journal: Embo J. / Year: 2002Title: Direct binding of ubiquitin conjugates by the mammalian p97 adapter complexes, p47 and ufd1-Npl4 Authors: Meyer, H.H. / Wang, Y. / Warren, G. | ||||||
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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 | 1nj3.cif.gz | 178.3 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1nj3.ent.gz | 145 KB | Display | PDB format |
| PDBx/mmJSON format | 1nj3.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nj/1nj3 ftp://data.pdbj.org/pub/pdb/validation_reports/nj/1nj3 | HTTPS FTP |
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-Related structure data
| Related structure data | |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 3376.865 Da / Num. of mol.: 1 / Fragment: NZF domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| #2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details | Contents: 1mM Npl4 NZF domain, U-15N,13C; 20 mM sodium Phosphate, pH 5.5, 50mM NaCl, 5 mM BME,90% H2O, 10% D2O Solvent system: 90% H2O/10% D2O |
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| Sample conditions | Ionic strength: 70 mM / pH: 5.5 / Pressure: ambient / Temperature: 291 K |
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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| Radiation wavelength | Relative weight: 1 | |||||||||||||||
| NMR spectrometer |
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Processing
| NMR software |
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| Refinement | Method: Torsion Angle Dynamics, Simulated annealing / Software ordinal: 1 Details: Inital structures from Torsion Angle Dynamics (DYANA) were regularized with a gentle annelaing protocol in CNS | ||||||||||||||||||||
| NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
| NMR ensemble | Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 20 |
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