- PDB-1fad: DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183 -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 1fad
Title
DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183
Components
PROTEIN (FADD PROTEIN)
Keywords
APOPTOSIS / FADD / DEATH DOMAIN
Function / homology
Function and homology information
TRAIL signaling / FasL/ CD95L signaling / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / TNFR1-induced proapoptotic signaling / Caspase activation via Death Receptors in the presence of ligand / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / negative regulation of activation-induced cell death of T cells / TRIF-mediated programmed cell death ...TRAIL signaling / FasL/ CD95L signaling / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / TNFR1-induced proapoptotic signaling / Caspase activation via Death Receptors in the presence of ligand / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / negative regulation of activation-induced cell death of T cells / TRIF-mediated programmed cell death / death-inducing signaling complex assembly / death effector domain binding / tumor necrosis factor receptor superfamily binding / caspase complex / CD95 death-inducing signaling complex / motor neuron apoptotic process / Regulation of necroptotic cell death / Regulation of TNFR1 signaling / TRAIL-activated apoptotic signaling pathway / caspase binding / ripoptosome / regulation of necroptotic process / positive regulation of macrophage differentiation / positive regulation of adaptive immune response / necroptotic signaling pathway / negative regulation of necroptotic process / death-inducing signaling complex / spleen development / T cell homeostasis / receptor serine/threonine kinase binding / positive regulation of type I interferon-mediated signaling pathway / tumor necrosis factor receptor binding / positive regulation of innate immune response / death receptor binding / lymph node development / cardiac muscle tissue development / positive regulation of activated T cell proliferation / positive regulation of extrinsic apoptotic signaling pathway / extrinsic apoptotic signaling pathway via death domain receptors / thymus development / positive regulation of proteolysis / T cell differentiation / extrinsic apoptotic signaling pathway in absence of ligand / T cell differentiation in thymus / positive regulation of execution phase of apoptosis / extrinsic apoptotic signaling pathway / kidney development / behavioral response to cocaine / signaling adaptor activity / apoptotic signaling pathway / positive regulation of T cell mediated cytotoxicity / positive regulation of interleukin-8 production / positive regulation of type II interferon production / cellular response to mechanical stimulus / positive regulation of tumor necrosis factor production / defense response to virus / protease binding / cell body / innate immune response / positive regulation of canonical NF-kappaB signal transduction / protein-macromolecule adaptor activity / apoptotic process / positive regulation of apoptotic process / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / identical protein binding / plasma membrane / cytosol / cytoplasm Similarity search - Function
FADD / : / Death effector domain / Death effector domain / Death effector domain (DED) profile. / Death effector domain / Death Domain, Fas / Death Domain, Fas / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). ...FADD / : / Death effector domain / Death effector domain / Death effector domain (DED) profile. / Death effector domain / Death Domain, Fas / Death Domain, Fas / Death domain profile. / DEATH domain, found in proteins involved in cell death (apoptosis). / Death domain / Death domain / Death-like domain superfamily / Orthogonal Bundle / Mainly Alpha Similarity search - Domain/homology
Mass: 11088.693 Da / Num. of mol.: 1 / Fragment: DEATH DOMAIN (RESIDUES 89-183) / Mutation: D96Y Source method: isolated from a genetically manipulated source Details: N-TERMINAL EXTENSION OF GLY-SER-HIS-MET FROM CLONING ARTIFACT. COORDINATES ARE NOT SHOWN FOR ARTIFACT. Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PET15B / Species (production host): Escherichia coli / Cellular location (production host): CYTOPLASM / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q61160
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
3D-15N-HSQC-NOESY
1
2
1
3D-13C
1
3
1
15N-EDITED NOESY
1
4
1
13C-(H)CCH-TOCSY
1
5
1
3D-15N-HSQC-TOCSY
1
6
1
NOESY
1
7
1
3D HNHA
NMR details
Text: DISTANCE CONSTRAINTS ARE DERIVED FROM THE 3D-13C, 15N-EDITED NOESY. J-COUPLING CONSTANTS FROM HNHA AND 13C CHEMICAL SHIFTS WERE USED AS CONTRAINTS. DURING THE REFINEMENT, DATABASE POTENTIAL WAS USED.
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