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- PDB-3c0z: Crystal structure of catalytic domain of human histone deacetylas... -

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Basic information

Entry
Database: PDB / ID: 3c0z
TitleCrystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with SAHA
ComponentsHistone deacetylase 7a
KeywordsHYDROLASE / HDAC / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / SGC / Alternative splicing / Chromatin regulator / Cytoplasm / Nucleus / Phosphoprotein / Polymorphism / Repressor / Transcription / Transcription regulation
Function / homology
Function and homology information


regulation of mRNA processing / histone deacetylase activity, hydrolytic mechanism / histone deacetylase / protein deacetylation / cell-cell junction assembly / SUMO transferase activity / negative regulation of non-canonical NF-kappaB signal transduction / positive regulation of cell migration involved in sprouting angiogenesis / protein lysine deacetylase activity / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides ...regulation of mRNA processing / histone deacetylase activity, hydrolytic mechanism / histone deacetylase / protein deacetylation / cell-cell junction assembly / SUMO transferase activity / negative regulation of non-canonical NF-kappaB signal transduction / positive regulation of cell migration involved in sprouting angiogenesis / protein lysine deacetylase activity / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / negative regulation of interleukin-2 production / histone deacetylase activity / Notch-HLH transcription pathway / histone deacetylase complex / protein sumoylation / negative regulation of osteoblast differentiation / vasculogenesis / SUMOylation of DNA damage response and repair proteins / 14-3-3 protein binding / protein kinase C binding / epigenetic regulation of gene expression / 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 / cytoplasm / cytosol
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
: / OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE / Histone deacetylase 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsMin, J. / Schuetz, A. / Loppnau, P. / Weigelt, J. / Sundstrom, M. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Plotnikov, A.N. / Structural Genomics Consortium (SGC)
CitationJournal: J.Biol.Chem. / Year: 2008
Title: Human HDAC7 harbors a class IIa histone deacetylase-specific zinc binding motif and cryptic deacetylase activity.
Authors: Schuetz, A. / Min, J. / Allali-Hassani, A. / Schapira, M. / Shuen, M. / Loppnau, P. / Mazitschek, R. / Kwiatkowski, N.P. / Lewis, T.A. / Maglathin, R.L. / McLean, T.H. / Bochkarev, A. / ...Authors: Schuetz, A. / Min, J. / Allali-Hassani, A. / Schapira, M. / Shuen, M. / Loppnau, P. / Mazitschek, R. / Kwiatkowski, N.P. / Lewis, T.A. / Maglathin, R.L. / McLean, T.H. / Bochkarev, A. / Plotnikov, A.N. / Vedadi, M. / Arrowsmith, C.H.
History
DepositionJan 21, 2008Deposition site: RCSB / Processing site: RCSB
SupersessionFeb 19, 2008ID: 2PQO
Revision 1.0Feb 19, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 30, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Histone deacetylase 7a
B: Histone deacetylase 7a
C: Histone deacetylase 7a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,97518
Polymers136,5553
Non-polymers1,42015
Water5,981332
1
A: Histone deacetylase 7a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,9926
Polymers45,5181
Non-polymers4735
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Histone deacetylase 7a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,9926
Polymers45,5181
Non-polymers4735
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Histone deacetylase 7a
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,9926
Polymers45,5181
Non-polymers4735
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)81.825, 81.825, 148.867
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 7a / HD7a / HDAC7


Mass: 45518.340 Da / Num. of mol.: 3 / Fragment: Catalytic domain: Residues 482-903
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HDAC7A, HDAC7 / Plasmid: pET28A-MHL / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q8WUI4
#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-SHH / OCTANEDIOIC ACID HYDROXYAMIDE PHENYLAMIDE / SAHA


Mass: 264.320 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C14H20N2O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 332 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.62 %
Crystal growTemperature: 300 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 20 % PEG 3350, 0.1 M HEPES pH 7.5, 10 % Isopropanol, VAPOR DIFFUSION, SITTING DROP, temperature 300K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 20, 2006
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. all: 60749 / Num. obs: 60749 / % possible obs: 93.5 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Rmerge(I) obs: 0.049 / Net I/σ(I): 23.8
Reflection shellResolution: 2.1→2.18 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.277 / Mean I/σ(I) obs: 3.7 / Num. unique all: 6428 / % possible all: 86.4

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
ARP/wARPmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 2NVR

2nvr
PDB Unreleased entry


Resolution: 2.1→40 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.937 / SU B: 5.826 / SU ML: 0.155 / Cross valid method: THROUGHOUT / ESU R: 0.268 / ESU R Free: 0.207 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24291 3080 5.1 %RANDOM
Rwork0.19664 ---
obs0.19903 57634 93.41 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 37.023 Å2
Baniso -1Baniso -2Baniso -3
1-1.67 Å20.83 Å20 Å2
2--1.67 Å20 Å2
3----2.5 Å2
Refinement stepCycle: LAST / Resolution: 2.1→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8400 0 37 332 8769
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0218657
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.7071.93611698
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.85851104
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.38323.782394
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.055151313
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.6841554
X-RAY DIFFRACTIONr_chiral_restr0.1230.21258
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.026705
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2250.24222
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3070.25749
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1790.2464
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.3380.210
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2360.284
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1470.217
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9961.55499
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.71528710
X-RAY DIFFRACTIONr_scbond_it2.63733182
X-RAY DIFFRACTIONr_scangle_it3.9724.52988
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.1→2.155 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.322 190 -
Rwork0.257 3775 -
obs--83.02 %

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