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Open data
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Basic information
Entry | Database: PDB / ID: 4rsu | ||||||
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Title | Crystal structure of the light and hvem complex | ||||||
![]() | (Tumor necrosis factor ...) x 2 | ||||||
![]() | IMMUNE SYSTEM / STRUCTURAL GENOMICS / PSI-BIOLOGY / NEW YORK STRUCTURAL GENOMICS / RESEARCH CONSORTIUM / NYSGRC / IMMUNITY / N-GLYCOSYLATION / MEMBRANE / SECRETED PROTEIN / CYTOKINE / IFN / JELLY-ROLL FOLD / Protein Structure Initiative / Atoms-to-Animals: The Immune Function Network / cysteine rich domain / signaling / cell membrane / secreted / New York Structural Genomics Research Consortium | ||||||
Function / homology | ![]() negative regulation of adaptive immune memory response / negative regulation of alpha-beta T cell proliferation / tumor necrosis factor receptor activity / positive regulation of cytokine production involved in immune response / 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 / Costimulation by the CD28 family ...negative regulation of adaptive immune memory response / negative regulation of alpha-beta T cell proliferation / tumor necrosis factor receptor activity / positive regulation of cytokine production involved in immune response / 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 / Costimulation by the CD28 family / positive regulation of myoblast fusion / T cell homeostasis / cytokine binding / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / positive regulation of T cell migration / positive regulation of myoblast differentiation / T cell proliferation / T cell costimulation / T cell activation / cytokine activity / TNFR2 non-canonical NF-kB pathway / cellular response to mechanical stimulus / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of peptidyl-tyrosine phosphorylation / virus receptor activity / defense response to Gram-negative bacterium / adaptive immune response / cell surface receptor signaling pathway / defense response to Gram-positive bacterium / immune response / external side of plasma membrane / innate immune response / signaling receptor binding / ubiquitin protein ligase binding / apoptotic process / signal transduction / extracellular space / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liu, W. / Ramagoal, U.A. / Himmel, D. / Bonanno, J.B. / Nathenson, S.G. / Almo, S.C. / Atoms-to-Animals: The Immune Function Network (IFN) / New York Structural Genomics Research Consortium (NYSGRC) | ||||||
![]() | ![]() Title: HVEM structures and mutants reveal distinct functions of binding to LIGHT and BTLA/CD160. Authors: Liu, W. / Chou, T.F. / Garrett-Thomson, S.C. / Seo, G.Y. / Fedorov, E. / Ramagopal, U.A. / Bonanno, J.B. / Wang, Q. / Kim, K. / Garforth, S.J. / Kakugawa, K. / Cheroutre, H. / Kronenberg, M. / Almo, S.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 561 KB | Display | ![]() |
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PDB format | ![]() | 463.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 7msgC ![]() 7msjC ![]() 4fhqS ![]() 4kg8S S: Starting model for refinement C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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Unit cell |
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Details | A LIGHT trimer binds to three HVEM. |
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Components
-Tumor necrosis factor ... , 2 types, 12 molecules ABCGHIDEFJKL
#1: Protein | Mass: 18188.549 Da / Num. of mol.: 6 / Fragment: EXTRACELLULAR DOMAIN, residues 83-240 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein | Mass: 14332.176 Da / Num. of mol.: 6 / Fragment: TNFR-Cys 1-3 repeats, residues 39-162 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Sugars , 1 types, 5 molecules ![](data/chem/img/NAG.gif)
#5: Sugar | ChemComp-NAG / |
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-Non-polymers , 3 types, 245 molecules ![](data/chem/img/CL.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-CL / #4: Chemical | ChemComp-GOL / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.65 Å3/Da / Density % sol: 53.65 % |
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Crystal grow | Temperature: 290 K / pH: 5.5 Details: 0.2M MAGNESIUM CHLORIDE, 0.1M BIS:TRIS BUFFER, 9% W/V PEG3350, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290.0K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 5, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.075 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. obs: 92792 / % possible obs: 99.9 % / Redundancy: 10.8 % / Rmerge(I) obs: 0.125 / Rsym value: 0.084 / Net I/σ(I): 21.7 |
Reflection shell | Resolution: 2.3→2.34 Å / Redundancy: 10.7 % / Rmerge(I) obs: 0.936 / Mean I/σ(I) obs: 3.1 / Rsym value: 0.818 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 4KG8, 4FHQ Resolution: 2.3→48.92 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.927 / SU B: 13.035 / SU ML: 0.149 / Cross valid method: THROUGHOUT / ESU R: 0.232 / ESU R Free: 0.196 / 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: 38.402 Å2
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Refinement step | Cycle: LAST / Resolution: 2.3→48.92 Å
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Refine LS restraints |
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