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- PDB-5kh3: Crystal structure of fragment (3-(5-Chloro-1,3-benzothiazol-2-yl)... -

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Basic information

Entry
Database: PDB / ID: 5kh3
TitleCrystal structure of fragment (3-(5-Chloro-1,3-benzothiazol-2-yl)propanoic acid) bound in the ubiquitin binding pocket of the HDAC6 zinc-finger domain
ComponentsHistone deacetylase 6
KeywordsHYDROLASE / HISTONE DEACETYLASE / HDAC / HDAC6 / FRAGMENT SCREENING / STRUCTURAL GENOMICS CONSORTIUM / SGC
Function / homology
Function and homology information


negative regulation of hydrogen peroxide metabolic process / cellular response to topologically incorrect protein / polyubiquitinated misfolded protein transport / positive regulation of cellular response to oxidative stress / erythrocyte enucleation / negative regulation of aggrephagy / 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 / positive regulation of cellular response to oxidative stress / erythrocyte enucleation / negative regulation of aggrephagy / positive regulation of cholangiocyte proliferation / response to misfolded protein / negative regulation of oxidoreductase activity / regulation of microtubule-based movement / type 2 mitophagy / negative regulation of protein-containing complex disassembly / negative regulation of axon extension involved in axon guidance / protein-containing complex disassembly / positive regulation of tubulin deacetylation / regulation of establishment of protein localization / regulation of autophagy of mitochondrion / tubulin deacetylation / Cilium Assembly / peptidyl-lysine deacetylation / collateral sprouting / tubulin deacetylase activity / Transcriptional regulation by RUNX2 / misfolded protein binding / lysosome localization / negative regulation of protein acetylation / negative regulation of microtubule depolymerization / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / cilium disassembly / protein deacetylation / response to growth factor / dendritic spine morphogenesis / histone deacetylase / regulation of androgen receptor signaling pathway / aggresome assembly / protein lysine deacetylase activity / positive regulation of signaling receptor activity / positive regulation of dendrite morphogenesis / cellular response to parathyroid hormone stimulus / cellular response to misfolded protein / aggresome / regulation of fat cell differentiation / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / microtubule associated complex / histone deacetylase activity / response to corticosterone / protein quality control for misfolded or incompletely synthesized proteins / dynein complex binding / negative regulation of gene expression, epigenetic / positive regulation of epithelial cell migration / Notch-HLH transcription pathway / axonal transport of mitochondrion / response to dexamethasone / cell leading edge / beta-tubulin binding / RUNX2 regulates osteoblast differentiation / histone deacetylase complex / polyubiquitin modification-dependent protein binding / response to immobilization stress / cilium assembly / HSF1 activation / alpha-tubulin binding / regulation of macroautophagy / negative regulation of protein-containing complex assembly / inclusion body / axon cytoplasm / response to amphetamine / multivesicular body / epigenetic regulation of gene expression / positive regulation of synaptic transmission, glutamatergic / transcription corepressor binding / ciliary basal body / ubiquitin binding / actin filament organization / regulation of autophagy / negative regulation of proteolysis / intracellular protein transport / protein destabilization / Late endosomal microautophagy / Hsp90 protein binding / regulation of protein stability / tau protein binding / caveola / NOTCH1 Intracellular Domain Regulates Transcription / beta-catenin binding / histone deacetylase binding / autophagy / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / cellular response to hydrogen peroxide / Aggrephagy / Chaperone Mediated Autophagy / protein polyubiquitination / positive regulation of peptidyl-serine phosphorylation / actin binding / cellular response to heat / microtubule binding / perikaryon / microtubule / RNA polymerase II cis-regulatory region sequence-specific DNA binding
Similarity search - Function
Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger / Zinc finger, UBP-type / Zn-finger in ubiquitin-hydrolases and other protein / Zinc finger UBP-type profile. / : / Histone deacetylase family / Histone deacetylase domain / Histone deacetylase domain superfamily / Histone deacetylase domain / Zinc/RING finger domain, C3HC4 (zinc finger) ...Ubiquitin Carboxyl-terminal Hydrolase-like zinc finger / Zinc finger, UBP-type / Zn-finger in ubiquitin-hydrolases and other protein / Zinc finger UBP-type profile. / : / Histone deacetylase family / Histone deacetylase domain / Histone deacetylase domain superfamily / Histone deacetylase domain / Zinc/RING finger domain, C3HC4 (zinc finger) / Ureohydrolase domain superfamily / Herpes Virus-1 / Zinc finger, RING/FYVE/PHD-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-6U6 / Histone deacetylase 6
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / Resolution: 1.6 Å
AuthorsHarding, R.J. / Dong, A. / Ravichandran, M. / Ferreira de Freitas, R. / Schapira, M. / Bountra, C. / Edwards, A.M. / Santhakumar, V. / Arrowsmith, C.M. / Structural Genomics Consortium (SGC)
CitationJournal: J. Med. Chem. / Year: 2017
Title: Small Molecule Antagonists of the Interaction between the Histone Deacetylase 6 Zinc-Finger Domain and Ubiquitin.
Authors: Harding, R.J. / Ferreira de Freitas, R. / Collins, P. / Franzoni, I. / Ravichandran, M. / Ouyang, H. / Juarez-Ornelas, K.A. / Lautens, M. / Schapira, M. / von Delft, F. / Santhakumar, V. / Arrowsmith, C.H.
History
DepositionJun 14, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 27, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2018Group: Database references / Derived calculations
Category: citation / citation_author / pdbx_struct_oper_list
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Feb 27, 2019Group: Data collection / Database references / Category: citation_author / Item: _citation_author.identifier_ORCID
Revision 1.3Sep 27, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / diffrn_radiation_wavelength / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Histone deacetylase 6
hetero molecules


Theoretical massNumber of molelcules
Total (without water)13,22118
Polymers11,9331
Non-polymers1,28817
Water1,47782
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area0 Å2
ΔGint0 kcal/mol
Surface area5980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)40.700, 44.027, 55.895
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Histone deacetylase 6 / HD6


Mass: 11932.607 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HDAC6, KIAA0901, JM21 / Plasmid: pET28-lic / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) codon plus / References: UniProt: Q9UBN7, histone deacetylase
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-UNX / UNKNOWN ATOM OR ION


Mass: 65.409 Da / Num. of mol.: 13 / Source method: obtained synthetically
#4: Chemical ChemComp-6U6 / 3-(5-chloranyl-1,3-benzothiazol-2-yl)propanoic acid


Mass: 241.694 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H8ClNO2S
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 82 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.1 Å3/Da / Density % sol: 41.38 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 4.6
Details: 2M Na-formate, 0.2M Na-acetate pH4.6, 5% ethylene glycol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU FR-E SUPERBRIGHT / Wavelength: 1.54178 Å
DetectorType: RIGAKU SATURN A200 / Detector: CCD / Date: Jun 6, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54178 Å / Relative weight: 1
ReflectionResolution: 1.6→34.61 Å / Num. obs: 13820 / % possible obs: 100 % / Redundancy: 6.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.064 / Rpim(I) all: 0.027 / Rrim(I) all: 0.07 / Net I/σ(I): 21.8 / Num. measured all: 93261
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allCC1/2Rpim(I) allRrim(I) all% possible all
1.6-1.636.50.4174.744496800.9170.1760.454100
8.76-29.894.90.02561.35331090.9990.0120.02898.4

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Processing

Software
NameVersionClassification
REFMAC5.8.0151refinement
Aimless0.5.26data scaling
PDB_EXTRACT3.2data extraction
XDSdata reduction
RefinementStarting model: pdbid 3C5K

3c5k


Resolution: 1.6→34.61 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.951 / SU B: 1.568 / SU ML: 0.054 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.082 / ESU R Free: 0.083 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: Amplitudes and unmerged intensities are included with this deposition. Diffraction images will be deposited in a public repository. Geometry restraints for the fragment candidate were prepared with GRADE.
RfactorNum. reflection% reflectionSelection details
Rfree0.1907 637 4.6 %RANDOM
Rwork0.1572 ---
obs0.1588 13143 99.91 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 58.55 Å2 / Biso mean: 15.362 Å2 / Biso min: 7.29 Å2
Baniso -1Baniso -2Baniso -3
1--0.18 Å20 Å20 Å2
2--1.25 Å2-0 Å2
3----1.06 Å2
Refinement stepCycle: final / Resolution: 1.6→34.61 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms782 0 31 86 899
Biso mean--23.43 25.85 -
Num. residues----101
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.019885
X-RAY DIFFRACTIONr_bond_other_d0.0030.02777
X-RAY DIFFRACTIONr_angle_refined_deg1.8511.9141222
X-RAY DIFFRACTIONr_angle_other_deg1.14131791
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4855111
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.33624.35939
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.42315118
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.567151
X-RAY DIFFRACTIONr_chiral_restr0.1230.2125
X-RAY DIFFRACTIONr_gen_planes_refined0.0110.0211105
X-RAY DIFFRACTIONr_gen_planes_other0.0030.02218
X-RAY DIFFRACTIONr_mcbond_it1.4261.383434
X-RAY DIFFRACTIONr_mcbond_other1.3391.37432
X-RAY DIFFRACTIONr_mcangle_it2.2792.058547
LS refinement shellResolution: 1.6→1.641 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.213 41 -
Rwork0.191 956 -
all-997 -
obs--100 %

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