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- PDB-2oq6: Crystal structure of JMJD2A complexed with histone H3 peptide tri... -

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Basic information

Entry
Database: PDB / ID: 2oq6
TitleCrystal structure of JMJD2A complexed with histone H3 peptide trimethylated at Lys9
Components
  • JmjC domain-containing histone demethylation protein 3A
  • synthetic peptidePeptide synthesis
KeywordsOXIDOREDUCTASE / double-stranded beta helix / demethylase / oxygenase / SGC / Structural Genomics / Structural Genomics Consortium
Function / homology
Function and homology information


histone H3-tri/dimethyl-lysine-36 demethylase activity / [histone H3]-trimethyl-L-lysine36 demethylase / histone demethylation / histone H3-K36 demethylation / histone H3-methyl-lysine-36 demethylase activity / cardiac muscle hypertrophy in response to stress / histone H3-tri/dimethyl-lysine-9 demethylase activity / [histone H3]-trimethyl-L-lysine9 demethylase / negative regulation of histone H3-K9 trimethylation / Chromatin modifying enzymes ...histone H3-tri/dimethyl-lysine-36 demethylase activity / [histone H3]-trimethyl-L-lysine36 demethylase / histone demethylation / histone H3-K36 demethylation / histone H3-methyl-lysine-36 demethylase activity / cardiac muscle hypertrophy in response to stress / histone H3-tri/dimethyl-lysine-9 demethylase activity / [histone H3]-trimethyl-L-lysine9 demethylase / negative regulation of histone H3-K9 trimethylation / Chromatin modifying enzymes / regulation of gene expression, epigenetic / histone H3-K9 demethylation / histone H3-methyl-lysine-9 demethylase activity / negative regulation of astrocyte differentiation / pericentric heterochromatin / telomere organization / Interleukin-7 signaling / histone demethylase activity / RNA Polymerase I Promoter Opening / DNA replication-dependent chromatin assembly / Assembly of the ORC complex at the origin of replication / DNA methylation / negative regulation of cell death / HCMV Late Events / SIRT1 negatively regulates rRNA expression / negative regulation of autophagy / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / Condensation of Prophase Chromosomes / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / PRC2 methylates histones and DNA / Defective pyroptosis / RNA Polymerase I Promoter Escape / HDACs deacetylate histones / methylated histone binding / nuclear chromosome / Transcriptional regulation by small RNAs / positive regulation of neuron differentiation / NoRC negatively regulates rRNA expression / Formation of the beta-catenin:TCF transactivating complex / response to nutrient levels / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / B-WICH complex positively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / RMTs methylate histone arginines / nucleosome assembly / HDMs demethylate histones / HCMV Early Events / Pre-NOTCH Transcription and Translation / Meiotic recombination / PKMTs methylate histone lysines / fibrillar center / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / nucleosome / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / chromatin remodeling / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / negative regulation of gene expression / negative regulation of transcription, DNA-templated / ubiquitin protein ligase binding / positive regulation of gene expression / protein-containing complex / DNA binding / extracellular exosome / zinc ion binding / membrane / extracellular region / nucleoplasm / nucleus / cytosol
Similarity search - Function
Jumonji domain-containing protein 2A Tudor domain / Lysine-specific demethylase 4, Tudor domain / Tudor domain / Tudor domain / JmjN domain / Small domain found in the jumonji family of transcription factors / JmjN domain profile. / jmjN domain / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. ...Jumonji domain-containing protein 2A Tudor domain / Lysine-specific demethylase 4, Tudor domain / Tudor domain / Tudor domain / JmjN domain / Small domain found in the jumonji family of transcription factors / JmjN domain profile. / jmjN domain / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. / Cupin / JmjC domain, hydroxylase / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain profile. / JmjC domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Core histone H2A/H2B/H3/H4 / Histone H2A/H2B/H3 / PHD zinc finger / Zinc finger, PHD-type / Histone-fold / Zinc finger, FYVE/PHD-type / Zinc finger, RING/FYVE/PHD-type / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Lysine-specific demethylase 4A / NICKEL (II) ION / N-OXALYLGLYCINE / Histone H3.1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsPilka, E.S. / Ng, S.S. / Kavanagh, K.L. / McDonough, M.A. / Savitsky, P. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A. / Sundstrom, M. ...Pilka, E.S. / Ng, S.S. / Kavanagh, K.L. / McDonough, M.A. / Savitsky, P. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A. / Sundstrom, M. / Schofield, C.J. / Oppermann, U. / Structural Genomics Consortium (SGC)
CitationJournal: Nature / Year: 2007
Title: Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Authors: Ng, S.S. / Kavanagh, K.L. / McDonough, M.A. / Butler, D. / Pilka, E.S. / Lienard, B.M. / Bray, J.E. / Savitsky, P. / Gileadi, O. / von Delft, F. / Rose, N.R. / Offer, J. / Scheinost, J.C. / ...Authors: Ng, S.S. / Kavanagh, K.L. / McDonough, M.A. / Butler, D. / Pilka, E.S. / Lienard, B.M. / Bray, J.E. / Savitsky, P. / Gileadi, O. / von Delft, F. / Rose, N.R. / Offer, J. / Scheinost, J.C. / Borowski, T. / Sundstrom, M. / Schofield, C.J. / Oppermann, U.
History
DepositionJan 31, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 13, 2007Provider: repository / Type: Initial release
Revision 1.1Oct 15, 2007Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Refinement description / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: JmjC domain-containing histone demethylation protein 3A
B: JmjC domain-containing histone demethylation protein 3A
C: synthetic peptide
D: synthetic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,97510
Polymers90,4334
Non-polymers5426
Water7,008389
1
A: JmjC domain-containing histone demethylation protein 3A
C: synthetic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,4885
Polymers45,2162
Non-polymers2713
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: JmjC domain-containing histone demethylation protein 3A
D: synthetic peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)45,4885
Polymers45,2162
Non-polymers2713
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)101.347, 149.880, 57.260
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

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Protein / Protein/peptide , 2 types, 4 molecules ABCD

#1: Protein JmjC domain-containing histone demethylation protein 3A / Jumonji domain-containing protein 2A


Mass: 44326.273 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: JMJD2A, JHDM3A, JMJD2, KIAA0677 / Plasmid: pNIC28-Bsa4 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3
References: UniProt: O75164, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
#2: Protein/peptide synthetic peptide / Peptide synthesis


Mass: 890.041 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: synthetic peptide / References: UniProt: P68431*PLUS

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Non-polymers , 4 types, 395 molecules

#3: Chemical ChemComp-NI / NICKEL (II) ION / Nickel


Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#5: Chemical ChemComp-OGA / N-OXALYLGLYCINE / N-Oxalylglycine


Mass: 147.086 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H5NO5 / Comment: inhibitor*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 389 / 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: 2.49 Å3/Da / Density % sol: 50.52 %
Crystal growTemperature: 277 K / pH: 5.5
Details: 0.1 M citrate, 4mM NiCl2, 20% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 277K, pH 5.50

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99991
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Dec 21, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99991 Å / Relative weight: 1
ReflectionResolution: 2→45.5 Å / Num. obs: 59834 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 5.6 % / Rmerge(I) obs: 0.085 / Rsym value: 0.094 / Net I/σ(I): 13.5
Reflection shellResolution: 2→2.11 Å / Redundancy: 5.5 % / Rmerge(I) obs: 0.837 / Mean I/σ(I) obs: 2.1 / Rsym value: 0.919 / % possible all: 99.7

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
MOSFLMdata reduction
CCP4(SCALA)data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→41.96 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.95 / SU B: 7.142 / SU ML: 0.103 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.144 / ESU R Free: 0.138 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20773 2514 4.2 %RANDOM
Rwork0.16286 ---
all0.16478 57260 --
obs0.16478 57260 99.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 33.18 Å2
Baniso -1Baniso -2Baniso -3
1--0.23 Å20 Å20 Å2
2---0.08 Å20 Å2
3---0.32 Å2
Refinement stepCycle: LAST / Resolution: 2→41.96 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5722 0 24 389 6135
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0225942
X-RAY DIFFRACTIONr_bond_other_d0.0010.024084
X-RAY DIFFRACTIONr_angle_refined_deg1.3491.9498067
X-RAY DIFFRACTIONr_angle_other_deg0.9223.0019884
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.2345718
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.77323.235272
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.97615952
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.2331533
X-RAY DIFFRACTIONr_chiral_restr0.0830.2837
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.026618
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021303
X-RAY DIFFRACTIONr_nbd_refined0.1970.21097
X-RAY DIFFRACTIONr_nbd_other0.1850.24022
X-RAY DIFFRACTIONr_nbtor_refined0.1830.22836
X-RAY DIFFRACTIONr_nbtor_other0.0850.22884
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1550.2315
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2260.28
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2270.227
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2650.26
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.56433722
X-RAY DIFFRACTIONr_mcbond_other1.00431429
X-RAY DIFFRACTIONr_mcangle_it4.55855758
X-RAY DIFFRACTIONr_scbond_it6.51472665
X-RAY DIFFRACTIONr_scangle_it8.393112304
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.05 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.309 174 -
Rwork0.249 4179 -
obs--99.43 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.3682-1.02420.54822.0508-0.62740.89730.16460.3660.0155-0.2981-0.27150.11360.05590.1330.1068-0.17090.03550.0079-0.0901-0.0052-0.1511-30.412-21.613-23.129
21.877-0.3721-0.12461.9384-0.4851.5930.0550.0302-0.0099-0.29710.0462-0.13660.2844-0.1194-0.1012-0.1056-0.0471-0.0425-0.15590.0063-0.0977-38.245-54.6292.169
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A8 - 355
2X-RAY DIFFRACTION2B7 - 354

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