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- PDB-1fad: DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183 -

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Basic information

Entry
Database: PDB / ID: 1fad
TitleDEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183
ComponentsPROTEIN (FADD PROTEIN)
KeywordsAPOPTOSIS / 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 / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / RIPK1-mediated regulated necrosis / Caspase activation via Death Receptors in the presence of ligand / TRIF-mediated programmed cell death / TNFR1-induced proapoptotic signaling ...TRAIL signaling / FasL/ CD95L signaling / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / positive regulation of CD8-positive, alpha-beta cytotoxic T cell extravasation / RIPK1-mediated regulated necrosis / Caspase activation via Death Receptors in the presence of ligand / TRIF-mediated programmed cell death / TNFR1-induced proapoptotic signaling / negative regulation of activation-induced cell death of T cells / death effector domain binding / CD95 death-inducing signaling complex / tumor necrosis factor receptor superfamily binding / ripoptosome / TRAIL-activated apoptotic signaling pathway / regulation of necroptotic process / positive regulation of adaptive immune response / positive regulation of macrophage differentiation / caspase binding / necroptotic signaling pathway / death-inducing signaling complex / negative regulation of necroptotic process / receptor serine/threonine kinase binding / activation of cysteine-type endopeptidase activity / response to morphine / cardiac muscle tissue development / 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 / positive regulation of activated T cell proliferation / T cell homeostasis / behavioral response to cocaine / positive regulation of proteolysis / T cell differentiation / lymph node development / extrinsic apoptotic signaling pathway / spleen development / extrinsic apoptotic signaling pathway in absence of ligand / thymus development / kidney development / positive regulation of interleukin-8 production / apoptotic signaling pathway / positive regulation of T cell mediated cytotoxicity / cellular response to mechanical stimulus / positive regulation of type II interferon production / positive regulation of tumor necrosis factor production / cell body / T cell differentiation in thymus / defense response to virus / positive regulation of canonical NF-kappaB signal transduction / protease binding / neuron projection / positive regulation of apoptotic process / membrane raft / innate immune response / apoptotic process / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / identical protein binding / nucleus / 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). / Death domain ...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
FAS-associated death domain protein
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMMULATED ANNEALING
AuthorsJeong, E.-J. / Bang, S. / Lee, T.H. / Park, Y.-I. / Sim, W.-S. / Kim, K.-S.
Citation
Journal: J.Biol.Chem. / Year: 1999
Title: The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
Authors: Jeong, E.J. / Bang, S. / Lee, T.H. / Park, Y.I. / Sim, W.S. / Kim, K.S.
#1: Journal: Mol.Cell.Biol. / Year: 1996
Title: A Mouse Fas-Associated Protein with Homology to the Human Mort1/FADD is Essential for Fas-Induced Apoptosis
Authors: Zhang, J. / Winoto, A.
History
DepositionMar 23, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Jul 6, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (FADD PROTEIN)


Theoretical massNumber of molelcules
Total (without water)11,0891
Polymers11,0891
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)21 / 50LOWEST ENERGY
RepresentativeModel #21

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Components

#1: Protein PROTEIN (FADD PROTEIN)


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

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D-15N-HSQC-NOESY
1213D-13C
13115N-EDITED NOESY
14113C-(H)CCH-TOCSY
1513D-15N-HSQC-TOCSY
161NOESY
1713D HNHA
NMR detailsText: 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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Sample preparation

DetailsContents: 2 MM
Sample conditionspH: 4.0 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYPLUS600VarianUNITYPLUS6005001
Varian INOVA500VarianINOVA5006002

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: DISTANCE GEOMETRY, SIMMULATED ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 21

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