+Open data
-Basic information
Entry | Database: PDB / ID: 1e3y | ||||||
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Title | Death domain from human FADD/MORT1 | ||||||
Components | FADD PROTEIN | ||||||
Keywords | APOPTOSIS / DEATH DOMAIN / ADAPTER MOLECULE / FAS RECEPTOR DEATH INDUCING SIGNALLING COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / negative regulation of activation-induced cell death of T cells / death effector domain binding / FasL/ CD95L signaling / tumor necrosis factor receptor superfamily binding / TRAIL signaling / CD95 death-inducing signaling complex / ripoptosome / TRAIL-activated apoptotic signaling pathway / death-inducing signaling complex assembly ...positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / negative regulation of activation-induced cell death of T cells / death effector domain binding / FasL/ CD95L signaling / tumor necrosis factor receptor superfamily binding / TRAIL signaling / CD95 death-inducing signaling complex / ripoptosome / TRAIL-activated apoptotic signaling pathway / death-inducing signaling complex assembly / Defective RIPK1-mediated regulated necrosis / TRIF-mediated programmed cell death / TLR3-mediated TICAM1-dependent programmed cell death / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / positive regulation of adaptive immune response / Caspase activation via Death Receptors in the presence of ligand / caspase binding / positive regulation of macrophage differentiation / necroptotic signaling pathway / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / death-inducing signaling complex / receptor serine/threonine kinase binding / negative regulation of necroptotic process / activation of cysteine-type endopeptidase activity / positive regulation of innate immune response / positive regulation of type I interferon-mediated signaling pathway / tumor necrosis factor receptor binding / death receptor binding / positive regulation of extrinsic apoptotic signaling pathway / motor neuron apoptotic process / TNFR1-induced proapoptotic signaling / RIPK1-mediated regulated necrosis / positive regulation of activated T cell proliferation / positive regulation of execution phase of apoptosis / T cell homeostasis / behavioral response to cocaine / positive regulation of proteolysis / extrinsic apoptotic signaling pathway via death domain receptors / lymph node development / signaling adaptor activity / extrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway in absence of ligand / spleen development / thymus development / kidney development / positive regulation of interleukin-8 production / apoptotic signaling pathway / Regulation of TNFR1 signaling / cellular response to mechanical stimulus / Regulation of necroptotic cell death / cytoplasmic side of plasma membrane / positive regulation of T cell mediated cytotoxicity / positive regulation of type II interferon production / positive regulation of tumor necrosis factor production / positive regulation of canonical NF-kappaB signal transduction / cell body / T cell differentiation in thymus / protease binding / defense response to virus / molecular adaptor activity / positive regulation of apoptotic process / innate immune response / protein-containing complex binding / apoptotic process / positive regulation of transcription by RNA polymerase II / identical protein binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | SOLUTION NMR / SIMULATED ANNEALING FROM RANDOM CHAIN STARTING CONFORMERS | ||||||
Model type details | MINIMIZED AVERAGE | ||||||
Authors | Driscoll, P.C. / Berglund, H. / Olerenshaw, D. / McDonald, N.Q. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: The Three-Dimensional Solution Structure and Dynamic Properties of the Human Fadd Death Domain Authors: Berglund, H. / Olerenshaw, D. / Sankar, A. / Federwisch, M. / Mcdonald, N.Q. / Driscoll, P.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1e3y.cif.gz | 46.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1e3y.ent.gz | 34.3 KB | Display | PDB format |
PDBx/mmJSON format | 1e3y.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1e3y_validation.pdf.gz | 336.7 KB | Display | wwPDB validaton report |
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Full document | 1e3y_full_validation.pdf.gz | 349.3 KB | Display | |
Data in XML | 1e3y_validation.xml.gz | 5.4 KB | Display | |
Data in CIF | 1e3y_validation.cif.gz | 6.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/e3/1e3y ftp://data.pdbj.org/pub/pdb/validation_reports/e3/1e3y | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11870.372 Da / Num. of mol.: 1 / Fragment: DEATH DOMAIN RESIDUES 93-192 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) Description: PCR CLONING INTO N-TERMINAL 6*HIS TAG THROMBIN-CLEAVABLE FUSION PROTEIN Plasmid: PET14B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q13158 |
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Compound details | CHIAN A EXTRA GLY-SER-HIS-MET- AT N-TERMINUS |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED FADD-DD. FULL DETAILS ARE GIVEN IN BERGLUND ET AL., J. MOL. BIOL. (2000), IN PRESS |
-Sample preparation
Sample conditions | Ionic strength: 50 MM PHOSPHATE BUFFER, 150MM NACL / pH: 6.2 / Pressure: 1 atm / Temperature: 298 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING FROM RANDOM CHAIN STARTING CONFORMERS Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION AND GOOD NON-BONDED CONTACTS Conformers calculated total number: 100 / Conformers submitted total number: 1 |