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- PDB-5edu: Crystal structure of human histone deacetylase 6 catalytic domain... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5edu | |||||||||
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Title | Crystal structure of human histone deacetylase 6 catalytic domain 2 in complex with trichostatin A | |||||||||
![]() | Maltose-binding periplasmic protein, Histone deacetylase 6 chimera | |||||||||
![]() | HYDROLASE/HYDROLASE INHIBITOR / HYDROLASE-HYDROLASE INHIBITOR complex | |||||||||
Function / homology | ![]() negative regulation of hydrogen peroxide metabolic process / cellular response to topologically incorrect protein / polyubiquitinated misfolded protein transport / negative regulation of aggrephagy / positive regulation of cellular response to oxidative stress / erythrocyte enucleation / positive regulation of cholangiocyte proliferation / response to misfolded protein / negative regulation of oxidoreductase activity / regulation of microtubule-based movement ...negative regulation of hydrogen peroxide metabolic process / cellular response to topologically incorrect protein / polyubiquitinated misfolded protein transport / negative regulation of aggrephagy / positive regulation of cellular response to oxidative stress / erythrocyte enucleation / positive regulation of cholangiocyte proliferation / response to misfolded protein / negative regulation of oxidoreductase activity / regulation of microtubule-based movement / parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization / negative regulation of protein-containing complex disassembly / protein-containing complex disassembly / negative regulation of axon extension involved in axon guidance / regulation of establishment of protein localization / positive regulation of tubulin deacetylation / tubulin deacetylation / Cilium Assembly / regulation of autophagy of mitochondrion / peptidyl-lysine deacetylation / tubulin deacetylase activity / collateral sprouting / Transcriptional regulation by RUNX2 / lysosome localization / negative regulation of protein acetylation / misfolded protein binding / negative regulation of microtubule depolymerization / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein deacetylation / cilium disassembly / response to growth factor / dendritic spine morphogenesis / histone deacetylase / aggresome assembly / regulation of androgen receptor signaling pathway / protein lysine deacetylase activity / positive regulation of signaling receptor activity / cellular response to misfolded protein / aggresome / cellular response to parathyroid hormone stimulus / positive regulation of dendrite morphogenesis / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / regulation of fat cell differentiation / microtubule associated complex / negative regulation of gene expression, epigenetic / histone deacetylase activity / response to corticosterone / dynein complex binding / detection of maltose stimulus / axonal transport of mitochondrion / maltose transport complex / Notch-HLH transcription pathway / response to dexamethasone / positive regulation of epithelial cell migration / beta-tubulin binding / cell leading edge / protein quality control for misfolded or incompletely synthesized proteins / RUNX2 regulates osteoblast differentiation / carbohydrate transport / histone deacetylase complex / carbohydrate transmembrane transporter activity / maltose binding / response to immobilization stress / alpha-tubulin binding / maltose transport / maltodextrin transmembrane transport / cilium assembly / polyubiquitin modification-dependent protein binding / HSF1 activation / regulation of macroautophagy / negative regulation of protein-containing complex assembly / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / inclusion body / axon cytoplasm / response to amphetamine / ATP-binding cassette (ABC) transporter complex / multivesicular body / positive regulation of synaptic transmission, glutamatergic / cell chemotaxis / transcription corepressor binding / ciliary basal body / ubiquitin binding / regulation of autophagy / caveola / negative regulation of proteolysis / actin filament organization / Late endosomal microautophagy / intracellular protein transport / Hsp90 protein binding / protein destabilization / regulation of protein stability / tau protein binding / NOTCH1 Intracellular Domain Regulates Transcription / beta-catenin binding / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / autophagy / histone deacetylase binding / Aggrephagy / Chaperone Mediated Autophagy Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Hai, Y. / Christianson, D.W. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Histone deacetylase 6 structure and molecular basis of catalysis and inhibition. Authors: Hai, Y. / Christianson, D.W. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 562.9 KB | Display | ![]() |
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PDB format | ![]() | 462.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 50 KB | Display | |
Data in CIF | ![]() | 68.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5eefC ![]() 5eeiC ![]() 5eekC ![]() 5eemC ![]() 5eenC ![]() 5ef7C ![]() 5ef8C ![]() 5efbC ![]() 5efgC ![]() 5efhC ![]() 5efjC ![]() 5efkC ![]() 5efnC ![]() 4cbtS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
-Protein / Sugars , 2 types, 4 molecules BA
#1: Protein | Mass: 81519.352 Da / Num. of mol.: 2 Fragment: MBP + HD6 catalytic domain 2 (UNP residues 479-835) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: malE, Z5632, ECs5017, HDAC6, KIAA0901, JM21 / Plasmid: pET28lic / Production host: ![]() ![]() References: UniProt: P0AEY0, UniProt: Q9UBN7, UniProt: P0AEX9*PLUS, histone deacetylase #2: Polysaccharide | |
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-Non-polymers , 4 types, 66 molecules ![](data/chem/img/TSN.gif)
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#3: Chemical | #4: Chemical | #5: Chemical | ChemComp-K / #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.44 Å3/Da / Density % sol: 49.49 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop / Details: 0.2 M potassium sodium tartrate, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 15, 2015 |
Radiation | Monochromator: single crystal Si(220) side bounce / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9798 Å / Relative weight: 1 |
Reflection | Resolution: 2.79→149 Å / Num. obs: 40864 / % possible obs: 100 % / Redundancy: 11 % / Rmerge(I) obs: 0.204 / Net I/σ(I): 12.9 |
Reflection shell | Highest resolution: 2.79 Å / Redundancy: 11.3 % / Rmerge(I) obs: 1.853 / Mean I/σ(I) obs: 1.9 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 4CBT Resolution: 2.79→87.54 Å / SU ML: 0.45 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.31 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.79→87.54 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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