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- PDB-3zns: HDAC7 bound with TFMO inhibitor tmp942 -

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Basic information

Entry
Database: PDB / ID: 3zns
TitleHDAC7 bound with TFMO inhibitor tmp942
ComponentsHISTONE DEACETYLASE 7
KeywordsHYDROLASE / ZBG / MBG
Function / homology
Function and homology information


regulation of mRNA processing / protein deacetylation / histone deacetylase / protein lysine deacetylase activity / negative regulation of non-canonical NF-kappaB signal transduction / cell-cell junction assembly / SUMO transferase activity / histone deacetylase activity / negative regulation of interleukin-2 production / positive regulation of cell migration involved in sprouting angiogenesis ...regulation of mRNA processing / protein deacetylation / histone deacetylase / protein lysine deacetylase activity / negative regulation of non-canonical NF-kappaB signal transduction / cell-cell junction assembly / SUMO transferase activity / histone deacetylase activity / negative regulation of interleukin-2 production / positive regulation of cell migration involved in sprouting angiogenesis / Notch-HLH transcription pathway / protein sumoylation / negative regulation of osteoblast differentiation / vasculogenesis / SUMOylation of DNA damage response and repair proteins / protein kinase C binding / 14-3-3 protein binding / Regulation of PTEN gene transcription / NOTCH1 Intracellular Domain Regulates Transcription / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / transcription corepressor activity / DNA-binding transcription factor binding / chromatin binding / protein kinase binding / negative regulation of transcription by RNA polymerase II / nucleoplasm / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
: / Histone deacetylase domain / Arginase; Chain A / Histone deacetylase family / Histone deacetylase domain / Histone deacetylase domain superfamily / Histone deacetylase domain / Ureohydrolase domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
: / Chem-NU7 / Histone deacetylase 7
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 Å
AuthorsLobera, M. / Madauss, K.P. / Pohlhaus, D.T. / Trump, R.P. / Nolan, M.A.
CitationJournal: Nat.Chem.Biol. / Year: 2013
Title: Selective Class Iia Histone Deacetylase Inhibition Via a Non-Chelating Zinc Binding Group
Authors: Lobera, M. / Madauss, K.P. / Pohlhaus, D.T. / Wright, Q.G. / Trocha, M. / Schmidt, D.R. / Baloglu, E. / Trump, R.P. / Head, M.S. / Hofmann, G.A. / Murray-Thompson, M. / Schwartz, B. / ...Authors: Lobera, M. / Madauss, K.P. / Pohlhaus, D.T. / Wright, Q.G. / Trocha, M. / Schmidt, D.R. / Baloglu, E. / Trump, R.P. / Head, M.S. / Hofmann, G.A. / Murray-Thompson, M. / Schwartz, B. / Chakravorty, S. / Wu, Z. / Mander, P.K. / Kruidenier, L. / Reid, R.A. / Burkhart, W. / Turunen, B.J. / Rong, J.X. / Wagner, C. / Moyer, M.B. / Wells, C. / Hong, X. / Moore, J.T. / Williams, J.D. / Soler, D. / Ghosh, S. / Nolan, M.A.
History
DepositionFeb 15, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 27, 2013Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2013Group: Database references
Revision 1.2May 1, 2013Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: HISTONE DEACETYLASE 7
B: HISTONE DEACETYLASE 7
C: HISTONE DEACETYLASE 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,76518
Polymers136,5553
Non-polymers2,21015
Water2,396133
1
A: HISTONE DEACETYLASE 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,2556
Polymers45,5181
Non-polymers7375
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: HISTONE DEACETYLASE 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,2556
Polymers45,5181
Non-polymers7375
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: HISTONE DEACETYLASE 7
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,2556
Polymers45,5181
Non-polymers7375
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)81.570, 81.570, 150.101
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32

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Components

#1: Protein HISTONE DEACETYLASE 7 / / HDAC7 / HD7 / HISTONE DEACETYLASE 7A / HD7A


Mass: 45518.340 Da / Num. of mol.: 3 / Fragment: CATALYTIC DOMAIN
Source method: isolated from a genetically manipulated source
Details: INHIBITOR / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q8WUI4, histone deacetylase
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: K
#4: Chemical ChemComp-NU7 / N-{[1-methyl-4-(4-phenyl-1,3-thiazol-2-yl)piperidin-4-yl]methyl}-3-[5-(trifluoromethyl)-1,2,4-oxadiazol-3-yl]benzamide


Mass: 527.561 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C26H24F3N5O2S
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 133 / 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: 2.11 Å3/Da / Density % sol: 41.74 % / Description: NONE
Crystal growpH: 7.4 / Details: 10% PEG 3350, 3% ISOPROPANAL, HEPES PH7.5, pH 7.4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97
DetectorType: MARRESEARCH MX-300 / Detector: CCD / Date: Mar 3, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 2.45→50 Å / Num. obs: 38814 / % possible obs: 99 % / Observed criterion σ(I): 2 / Redundancy: 5.9 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 30.3
Reflection shellResolution: 2.45→2.49 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 3.6 / % possible all: 99

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Processing

Software
NameVersionClassification
REFMAC5.5.0053refinement
HKLdata reduction
HKLdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.45→70.71 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.939 / SU B: 20.711 / SU ML: 0.21 / Cross valid method: THROUGHOUT / ESU R: 0.649 / ESU R Free: 0.264 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.22496 2054 5 %RANDOM
Rwork0.18619 ---
obs0.18814 38814 99.78 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 26.288 Å2
Baniso -1Baniso -2Baniso -3
1-2.16 Å21.08 Å20 Å2
2--2.16 Å20 Å2
3----3.24 Å2
Refinement stepCycle: LAST / Resolution: 2.45→70.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8345 0 123 133 8601
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0218669
X-RAY DIFFRACTIONr_bond_other_d0.0010.025693
X-RAY DIFFRACTIONr_angle_refined_deg0.9641.94911785
X-RAY DIFFRACTIONr_angle_other_deg0.801313813
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.25351101
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.06623.789388
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.883151290
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.6771552
X-RAY DIFFRACTIONr_chiral_restr0.0530.21263
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0219915
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021804
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.2081.55463
X-RAY DIFFRACTIONr_mcbond_other0.0321.52275
X-RAY DIFFRACTIONr_mcangle_it0.39528675
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it0.57433206
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.9524.53110
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.452→2.516 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.274 163 -
Rwork0.237 2861 -
obs--99.31 %

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