+Open data
-Basic information
Entry | Database: PDB / ID: 4j6g | |||||||||
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Title | CRYSTAL STRUCTURE OF LIGHT AND DcR3 COMPLEX | |||||||||
Components | (Tumor necrosis factor ...) x 2 | |||||||||
Keywords | IMMUNE SYSTEM / LIGHT / DCR3 / TNF / TNFR / TNF14 / STRUCTURAL GENOMICS / PSI-BIOLOGY / NEW HVEM / N-GLYCOSYLATION / MEMBRANE / SECRETED PROTEIN / CYTOKINE / IFN / JELLY-ROLL FOLD / BIND TNF RECEPTOR HVEM AND LTBR / LTBR / Protein Structure Initiative / Atoms-to-Animals: The Immune Function Network / New York Structural Genomics Research Consortium / NYSGRC | |||||||||
Function / homology | Function and homology information TNFs bind their physiological receptors / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / positive regulation of T cell chemotaxis / T cell chemotaxis / tumor necrosis factor receptor binding / positive regulation of myoblast fusion / T cell homeostasis / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / positive regulation of myoblast differentiation / T cell proliferation ...TNFs bind their physiological receptors / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / positive regulation of T cell chemotaxis / T cell chemotaxis / tumor necrosis factor receptor binding / positive regulation of myoblast fusion / T cell homeostasis / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / positive regulation of myoblast differentiation / T cell proliferation / T cell costimulation / T cell activation / cytokine activity / TNFR2 non-canonical NF-kB pathway / positive regulation of non-canonical NF-kappaB signal transduction / cellular response to mechanical stimulus / signaling receptor activity / immune response / signaling receptor binding / apoptotic process / negative regulation of apoptotic process / signal transduction / extracellular space / extracellular region / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | |||||||||
Authors | Liu, W. / Zhan, C. / Bonanno, J.B. / Bhosle, R.C. / Nathenson, S.G. / Almo, S.C. / Atoms-to-Animals: The Immune Function Network (IFN) / New York Structural Genomics Research Consortium (NYSGRC) | |||||||||
Citation | Journal: Structure / Year: 2014 Title: Mechanistic basis for functional promiscuity in the TNF and TNF receptor superfamilies: structure of the LIGHT:DcR3 assembly. Authors: Liu, W. / Zhan, C. / Cheng, H. / Kumar, P.R. / Bonanno, J.B. / Nathenson, S.G. / Almo, S.C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4j6g.cif.gz | 134.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4j6g.ent.gz | 103.1 KB | Display | PDB format |
PDBx/mmJSON format | 4j6g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j6/4j6g ftp://data.pdbj.org/pub/pdb/validation_reports/j6/4j6g | HTTPS FTP |
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-Related structure data
Related structure data | 4en0SC 4kg8C 4kggC 4kgqC S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
-Tumor necrosis factor ... , 2 types, 4 molecules ABCD
#1: Protein | Mass: 18188.549 Da / Num. of mol.: 2 / Fragment: UNP residues 83-240 / Mutation: K214E Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNFSF14, HVEML, LIGHT, UNQ391/PRO726 / Production host: Drosophila (fruit flies) / References: UniProt: O43557 #2: Protein | Mass: 19044.217 Da / Num. of mol.: 2 / Fragment: UNP residues 30-195 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: TNFRSF6B, DCR3, TR6, UNQ186/PRO212 / Production host: Drosophila (fruit flies) / References: UniProt: O95407 |
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-Sugars , 2 types, 2 molecules
#3: Polysaccharide | alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
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#6: Sugar | ChemComp-NAG / |
-Non-polymers , 3 types, 50 molecules
#4: Chemical | #5: Chemical | #7: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.71 Å3/Da / Density % sol: 66.81 % |
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Crystal grow | Temperature: 290 K / Method: vapor diffusion, sitting drop / pH: 5.5 Details: 0.2M SODIUM CHLORIDE, 0.1M SODIUM CITRATE:CITRIC ACID BUFFER 1.0M AMMONIUM PHOSPHATE DIBASIC, PH5.5,, VAPOR DIFFUSION, SITTING DROP, temperature 290K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.075 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 2, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.075 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→50 Å / Num. obs: 43288 / % possible obs: 100 % / Redundancy: 11.2 % / Rmerge(I) obs: 0.102 / Rsym value: 0.077 / Net I/σ(I): 27.2 |
Reflection shell | Resolution: 2.4→2.44 Å / Redundancy: 11.2 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 3.5 / Rsym value: 0.774 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4EN0 Resolution: 2.4→19.93 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.922 / SU B: 5.459 / SU ML: 0.128 / Cross valid method: THROUGHOUT / ESU R: 0.22 / ESU R Free: 0.193 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 41.906 Å2
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Refinement step | Cycle: LAST / Resolution: 2.4→19.93 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.402→2.464 Å / Total num. of bins used: 20
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