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- PDB-1vkg: Crystal Structure of Human HDAC8 complexed with CRA-19156 -

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Basic information

Entry
Database: PDB / ID: 1vkg
TitleCrystal Structure of Human HDAC8 complexed with CRA-19156
ComponentsHistone deacetylase 8
KeywordsHYDROLASE / histone deacetylase / zinc hydrolase
Function / homology
Function and homology information


histone decrotonylase activity / histone deacetylase / protein lysine deacetylase activity / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / regulation of telomere maintenance / mitotic sister chromatid cohesion / histone deacetylase activity / nuclear chromosome / Notch-HLH transcription pathway / histone deacetylase complex ...histone decrotonylase activity / histone deacetylase / protein lysine deacetylase activity / Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In linear amides / regulation of telomere maintenance / mitotic sister chromatid cohesion / histone deacetylase activity / nuclear chromosome / Notch-HLH transcription pathway / histone deacetylase complex / negative regulation of protein ubiquitination / Resolution of Sister Chromatid Cohesion / Hsp70 protein binding / epigenetic regulation of gene expression / HDACs deacetylate histones / Hsp90 protein binding / regulation of protein stability / NOTCH1 Intracellular Domain Regulates Transcription / Constitutive Signaling by NOTCH1 PEST Domain Mutants / Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants / Separation of Sister Chromatids / chromatin organization / DNA-binding transcription factor binding / negative regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / metal ion binding / cytoplasm
Similarity search - Function
Histone deacetylase / 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-CRI / Histone deacetylase 8
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsSomoza, J.R. / Skene, R.J. / Katz, B.A. / Mol, C. / Ho, J.D. / Jennings, A.J. / Luong, C. / Arvai, A. / Buggy, J.J. / Chi, E. ...Somoza, J.R. / Skene, R.J. / Katz, B.A. / Mol, C. / Ho, J.D. / Jennings, A.J. / Luong, C. / Arvai, A. / Buggy, J.J. / Chi, E. / Tang, J. / Sang, B.-C. / Verner, E. / Wynands, R. / Leahy, E.M. / Dougan, D.R. / Snell, G. / Navre, M. / Knuth, M.W. / Swanson, R.V. / McRee, D.E. / Tari, L.W.
CitationJournal: Structure / Year: 2004
Title: Structural Snapshots of Human HDAC8 Provide Insights into the Class I Histone Deacetylases
Authors: Somoza, J.R. / Skene, R.J. / Katz, B.A. / Mol, C. / Ho, J.D. / Jennings, A.J. / Luong, C. / Arvai, A. / Buggy, J.J. / Chi, E. / Tang, J. / Sang, B.-C. / Verner, E. / Wynands, R. / Leahy, E.M. ...Authors: Somoza, J.R. / Skene, R.J. / Katz, B.A. / Mol, C. / Ho, J.D. / Jennings, A.J. / Luong, C. / Arvai, A. / Buggy, J.J. / Chi, E. / Tang, J. / Sang, B.-C. / Verner, E. / Wynands, R. / Leahy, E.M. / Dougan, D.R. / Snell, G. / Navre, M. / Knuth, M.W. / Swanson, R.V. / McRee, D.E. / Tari, L.W.
History
DepositionMay 13, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 27, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 23, 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_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_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

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Assembly

Deposited unit
A: Histone deacetylase 8
B: Histone deacetylase 8
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,6178
Polymers83,6052
Non-polymers1,0126
Water4,396244
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3560 Å2
ΔGint-109 kcal/mol
Surface area25880 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.63, 92.71, 98.76
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Histone deacetylase 8 / HDAC8


Mass: 41802.477 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: HDAC8, HDACL1 / Plasmid: pFastbacHTa / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9 / References: UniProt: Q9BY41
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-CRI / 5-(4-METHYL-BENZOYLAMINO)-BIPHENYL-3,4'-DICARBOXYLIC ACID 3-DIMETHYLAMIDE-4'-HYDROXYAMIDE


Mass: 417.457 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H23N3O4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 244 / 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: 2.26 Å3/Da / Density % sol: 45.61 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: PEG 3350, 0.2M KCl, pH 6.8-7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RUH3R / Wavelength: 1.5418
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Dec 5, 2002 / Details: osmic
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.2→27.74 Å / Num. all: 39198 / Num. obs: 37725 / % possible obs: 96.24 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.8 % / Rmerge(I) obs: 0.092 / Rsym value: 0.092 / Net I/σ(I): 6.4
Reflection shellResolution: 2.2→2.3 Å / Rmerge(I) obs: 0.342 / Mean I/σ(I) obs: 1.7 / Num. unique all: 4695 / Rsym value: 0.342 / % possible all: 80.7

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Processing

Software
NameVersionClassification
Crystaldata collection
Crystaldata reduction
X-sightmodel building
X-PLOR3.851refinement
CrystalClear(MSC/RIGAKU)data scaling
X-SIGHTphasing
X-PLOR3.851refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1T64

1t64


Resolution: 2.2→7 Å / Cross valid method: THROUGHOUT / σ(F): 1.1 / σ(I): 0 / Stereochemistry target values: RESIDUAL
RfactorNum. reflection% reflectionSelection details
Rfree0.304 1872 5 %RANDOM
Rwork0.237 ---
all-37437 --
obs-34275 90.5 %-
Refinement stepCycle: LAST / Resolution: 2.2→7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10798 0 110 733 11641
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.018
X-RAY DIFFRACTIONx_angle_deg3.8
LS refinement shellResolution: 2.2→2.3 Å / Total num. of bins used: 10 /
RfactorNum. reflection
Rfree0.404 202
Rwork0.389 3650

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