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Open data
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Basic information
Entry | Database: PDB / ID: 5ypa | ||||||
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Title | p62/SQSTM1 ZZ domain with Lys-peptide | ||||||
![]() | 78 kDa glucose-regulated protein,Sequestosome-1 | ||||||
![]() | SIGNALING PROTEIN / Complex / p62/SQSTM1 / ZZ domain / Autophagy / N-end rule | ||||||
Function / homology | ![]() regulation of protein folding in endoplasmic reticulum / regulation of ATF6-mediated unfolded protein response / regulation of PERK-mediated unfolded protein response / cerebellum structural organization / ATF6 (ATF6-alpha) activates chaperones / ATF6B (ATF6-beta) activates chaperones / brown fat cell proliferation / protein localization to perinuclear region of cytoplasm / maintenance of protein localization in endoplasmic reticulum / negative regulation of IRE1-mediated unfolded protein response ...regulation of protein folding in endoplasmic reticulum / regulation of ATF6-mediated unfolded protein response / regulation of PERK-mediated unfolded protein response / cerebellum structural organization / ATF6 (ATF6-alpha) activates chaperones / ATF6B (ATF6-beta) activates chaperones / brown fat cell proliferation / protein localization to perinuclear region of cytoplasm / maintenance of protein localization in endoplasmic reticulum / negative regulation of IRE1-mediated unfolded protein response / regulation of Ras protein signal transduction / protein targeting to vacuole involved in autophagy / IRE1alpha activates chaperones / cerebellar Purkinje cell layer development / Lewy body / ATF6 (ATF6-alpha) activates chaperone genes / regulation of IRE1-mediated unfolded protein response / response to mitochondrial depolarisation / aggrephagy / endoplasmic reticulum chaperone complex / amphisome / PERK regulates gene expression / negative regulation of toll-like receptor 4 signaling pathway / protein folding in endoplasmic reticulum / pexophagy / regulation of protein complex stability / autophagy of mitochondrion / endosome organization / non-membrane-bounded organelle assembly / molecular sequestering activity / misfolded protein binding / post-translational protein targeting to membrane, translocation / phagophore assembly site / regulation of mitochondrion organization / aggresome / regulation of canonical NF-kappaB signal transduction / ubiquitin-modified protein reader activity / Nuclear events mediated by NFE2L2 / autolysosome / K63-linked polyubiquitin modification-dependent protein binding / intracellular non-membrane-bounded organelle / endosomal transport / temperature homeostasis / immune system process / ER overload response / non-chaperonin molecular chaperone ATPase / mitophagy / chaperone cofactor-dependent protein refolding / endoplasmic reticulum-Golgi intermediate compartment / Regulation of HSF1-mediated heat shock response / autophagosome / cellular response to interleukin-4 / negative regulation of protein-containing complex assembly / cellular response to glucose starvation / positive regulation of autophagy / energy homeostasis / signaling adaptor activity / ERAD pathway / protein folding chaperone / endoplasmic reticulum unfolded protein response / inclusion body / sperm midpiece / negative regulation of protein ubiquitination / heat shock protein binding / protein sequestering activity / substantia nigra development / p75NTR recruits signalling complexes / PINK1-PRKN Mediated Mitophagy / Pexophagy / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / sarcomere / response to endoplasmic reticulum stress / SH2 domain binding / molecular condensate scaffold activity / ubiquitin binding / positive regulation of protein ubiquitination / positive regulation of long-term synaptic potentiation / response to ischemia / macroautophagy / protein kinase C binding / positive regulation of protein localization to plasma membrane / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ATP-dependent protein folding chaperone / negative regulation of transforming growth factor beta receptor signaling pathway / ionotropic glutamate receptor binding / P-body / protein catabolic process / protein localization / receptor tyrosine kinase binding / PML body / autophagy / Interleukin-1 signaling / protein import into nucleus / KEAP1-NFE2L2 pathway / Signaling by ALK fusions and activated point mutants / unfolded protein binding / melanosome / late endosome / Platelet degranulation Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kwon, D.H. / Kim, L. / Song, H.K. | ||||||
![]() | ![]() Title: Insights into degradation mechanism of N-end rule substrates by p62/SQSTM1 autophagy adapter. Authors: Kwon, D.H. / Park, O.H. / Kim, L. / Jung, Y.O. / Park, Y. / Jeong, H. / Hyun, J. / Kim, Y.K. / Song, H.K. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.5 KB | Display | ![]() |
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PDB format | ![]() | 34.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 418.3 KB | Display | ![]() |
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Full document | ![]() | 418.3 KB | Display | |
Data in XML | ![]() | 6 KB | Display | |
Data in CIF | ![]() | 7.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5yp7C ![]() 5yp8C ![]() 5ypbC ![]() 5ypcC ![]() 5ypeC ![]() 5ypfC ![]() 5ypgC ![]() 5yphC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 6485.300 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ZN / #3: Water | ChemComp-HOH / | Sequence details | LYS (-3 position) is synthetic residue generated by special enzyme | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.65 Å3/Da / Density % sol: 25.51 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: PEG 8000, CaCl2, HEPES |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 17, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.2 Å / Relative weight: 1 |
Reflection | Resolution: 2.502→21.993 Å / Num. obs: 2939 / % possible obs: 96.1 % / Redundancy: 4.5 % / Net I/σ(I): 13 |
Reflection shell | Resolution: 2.5→2.54 Å |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.502→21.993 Å
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Refine LS restraints |
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LS refinement shell |
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