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Yorodumi- PDB-1l0a: DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3 -
+Open data
-Basic information
Entry | Database: PDB / ID: 1l0a | ||||||
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Title | DOWNSTREAM REGULATOR TANK BINDS TO THE CD40 RECOGNITION SITE ON TRAF3 | ||||||
Components |
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Keywords | SIGNALING PROTEIN / CD40 / NF-kB signaling / TANK / TNF receptor / TRAF3 | ||||||
Function / homology | Function and homology information regulation of interferon-beta production / positive regulation of protein deubiquitination / TRAF3 deficiency - HSE / positive regulation of ubiquitin-specific protease activity / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / Toll signaling pathway / serine/threonine protein kinase complex / CD40 receptor complex / TRIF-dependent toll-like receptor signaling pathway / regulation of defense response to virus ...regulation of interferon-beta production / positive regulation of protein deubiquitination / TRAF3 deficiency - HSE / positive regulation of ubiquitin-specific protease activity / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / Toll signaling pathway / serine/threonine protein kinase complex / CD40 receptor complex / TRIF-dependent toll-like receptor signaling pathway / regulation of defense response to virus / regulation of proteolysis / thioesterase binding / tumor necrosis factor receptor binding / deubiquitinase activator activity / regulation of canonical NF-kappaB signal transduction / TRAF6 mediated IRF7 activation / toll-like receptor 4 signaling pathway / negative regulation of NF-kappaB transcription factor activity / toll-like receptor signaling pathway / type I interferon-mediated signaling pathway / molecular function inhibitor activity / positive regulation of type I interferon production / protein K63-linked ubiquitination / cellular response to interleukin-1 / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of canonical NF-kappaB signal transduction / ubiquitin ligase complex / tumor necrosis factor-mediated signaling pathway / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / regulation of cytokine production / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / TICAM1-dependent activation of IRF3/IRF7 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / TNFR2 non-canonical NF-kB pathway / Negative regulators of DDX58/IFIH1 signaling / cellular response to ionizing radiation / RING-type E3 ubiquitin transferase / cytoplasmic side of plasma membrane / ubiquitin-protein transferase activity / SARS-CoV-1 activates/modulates innate immune responses / ubiquitin protein ligase activity / Ovarian tumor domain proteases / cellular response to tumor necrosis factor / TRAF3-dependent IRF activation pathway / defense response to virus / protein phosphatase binding / regulation of apoptotic process / molecular adaptor activity / endosome membrane / endosome / DNA damage response / ubiquitin protein ligase binding / apoptotic process / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / signal transduction / protein-containing complex / mitochondrion / zinc ion binding / identical protein binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.9 Å | ||||||
Authors | Li, C. / Ni, C.-Z. / Havert, M.L. / Cabezas, E. / He, J. / Kaiser, D. / Reed, J.C. / Satterthwait, A.C. / Cheng, G. / Ely, K.R. | ||||||
Citation | Journal: Structure / Year: 2002 Title: Downstream regulator TANK binds to the CD40 recognition site on TRAF3. Authors: Li, C. / Ni, C.Z. / Havert, M.L. / Cabezas, E. / He, J. / Kaiser, D. / Reed, J.C. / Satterthwait, A.C. / Cheng, G. / Ely, K.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1l0a.cif.gz | 54.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1l0a.ent.gz | 39.1 KB | Display | PDB format |
PDBx/mmJSON format | 1l0a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1l0a_validation.pdf.gz | 430.3 KB | Display | wwPDB validaton report |
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Full document | 1l0a_full_validation.pdf.gz | 438.4 KB | Display | |
Data in XML | 1l0a_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 1l0a_validation.cif.gz | 13.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l0/1l0a ftp://data.pdbj.org/pub/pdb/validation_reports/l0/1l0a | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 21833.135 Da / Num. of mol.: 1 / Fragment: Residues 377-568 / Mutation: T195K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q13114 |
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#2: Protein/peptide | Mass: 2054.343 Da / Num. of mol.: 1 / Fragment: Residues 178-195 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q92844 |
#3: 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: 3.19 Å3/Da / Density % sol: 61.46 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.8 Details: 100mM MES, 15% PEG1000, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystal grow | *PLUS Details: unpublished data |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-1 / Wavelength: 0.97 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 15, 2000 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.9→50 Å / Num. all: 7076 / Num. obs: 7042 / % possible obs: 99.5 % / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.9→2.98 Å / Redundancy: 5.5 % / % possible all: 100 |
Reflection | *PLUS Num. obs: 7263 / Num. measured all: 38649 / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.9→50 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 37.3 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→50 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.23 / Rfactor Rfree: 0.295 / Rfactor Rwork: 0.23 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |