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- PDB-3n9o: ceKDM7A from C.elegans, complex with H3K4me3 peptide, H3K9me2 pep... -

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Basic information

Entry
Database: PDB / ID: 3n9o
TitleceKDM7A from C.elegans, complex with H3K4me3 peptide, H3K9me2 peptide and NOG
Components
  • (Histone H3 peptide) x 2
  • Putative uncharacterized protein
KeywordsOXIDOREDUCTASE / Histone / methylation / demethylase / PHD / JmjC / Fe(II) and alpha-KG (alpha-ketoglutarate)-dependent dioxygenase family
Function / homology
Function and homology information


HDMs demethylate histones / histone H3K27me2/H3K27me3 demethylase activity / 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 / histone H3K9 demethylase activity / histone demethylase activity / methylated histone binding / transcription coregulator activity / structural constituent of chromatin / nucleosome / histone binding ...HDMs demethylate histones / histone H3K27me2/H3K27me3 demethylase activity / 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 / histone H3K9 demethylase activity / histone demethylase activity / methylated histone binding / transcription coregulator activity / structural constituent of chromatin / nucleosome / histone binding / protein heterodimerization activity / regulation of transcription by RNA polymerase II / DNA binding / metal ion binding / nucleus
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #1360 / Jumonji, helical domain / Jumonji helical domain / Zinc/RING finger domain, C3HC4 (zinc finger) / Cupin / Herpes Virus-1 / JmjC domain, hydroxylase / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain / JmjC domain profile. ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #1360 / Jumonji, helical domain / Jumonji helical domain / Zinc/RING finger domain, C3HC4 (zinc finger) / Cupin / Herpes Virus-1 / JmjC domain, hydroxylase / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain / JmjC domain profile. / Zinc finger, PHD-type, conserved site / Zinc finger PHD-type signature. / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Histone H3 signature 1. / Zinc finger, PHD-type / PHD zinc finger / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Zinc finger, FYVE/PHD-type / Histone-fold / Zinc finger, RING/FYVE/PHD-type / Jelly Rolls / Up-down Bundle / Sandwich / 2-Layer Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
: / N-OXALYLGLYCINE / Histone H3 / Lysine-specific demethylase 7 homolog
Similarity search - Component
Biological speciesCaenorhabditis elegans (invertebrata)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.309 Å
AuthorsYang, Y. / Hu, L. / Wang, P. / Hou, H. / Chen, C.D. / Xu, Y.
CitationJournal: Cell Res. / Year: 2010
Title: Structural insights into a dual-specificity histone demethylase ceKDM7A from Caenorhabditis elegans
Authors: Yang, Y. / Hu, L. / Wang, P. / Hou, H. / Lin, Y. / Liu, Y. / Li, Z. / Gong, R. / Feng, X. / Zhou, L. / Zhang, W. / Dong, Y. / Yang, H. / Lin, H. / Wang, Y. / Chen, C.D. / Xu, Y.
History
DepositionMay 31, 2010Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jun 30, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 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.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.pdbx_leaving_atom_flag / _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_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: Putative uncharacterized protein
B: Histone H3 peptide
C: Histone H3 peptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,7347
Polymers65,4013
Non-polymers3344
Water4,990277
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2680 Å2
ΔGint-8 kcal/mol
Surface area23250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.090, 87.379, 102.727
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 1 molecules A

#1: Protein Putative uncharacterized protein / lysine demethylase


Mass: 61945.496 Da / Num. of mol.: 1 / Fragment: PHD domain, UNP residues 201-724
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Caenorhabditis elegans (invertebrata) / Gene: F29B9.2 / Plasmid: pET15b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q9GYI0, [histone H3]-dimethyl-L-lysine36 demethylase

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Protein/peptide , 2 types, 2 molecules BC

#2: Protein/peptide Histone H3 peptide


Mass: 1607.877 Da / Num. of mol.: 1 / Fragment: JMJC domain, UNP residues 2-16 / Source method: obtained synthetically / Details: chemical synthesis, purchased from a company / Source: (synth.) Caenorhabditis elegans (invertebrata) / References: UniProt: P08898
#3: Protein/peptide Histone H3 peptide


Mass: 1847.152 Da / Num. of mol.: 1 / Fragment: JMJC domain, UNP residues 2-18 / Source method: obtained synthetically / Details: chemical synthesis, purchased from a company / Source: (synth.) Caenorhabditis elegans (invertebrata) / References: UniProt: P08898

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Non-polymers , 4 types, 281 molecules

#4: Chemical ChemComp-FE2 / FE (II) ION


Mass: 55.845 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe
#5: Chemical ChemComp-ZN / ZINC ION


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


Mass: 147.086 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H5NO5 / Comment: inhibitor*YM
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 277 / 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: 2.37 Å3/Da / Density % sol: 48.11 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 16% PEG 3350, 0.2M Sodium Fluoride, 0.1M Bis-Tris or HEPES, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U / Wavelength: 1.2828 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: May 6, 2009
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2828 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 27497 / % possible obs: 98.4 % / Biso Wilson estimate: 39.49 Å2
Reflection shellResolution: 2.3→2.38 Å / % possible all: 87.3

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3N9M

3n9m


Resolution: 2.309→44.28 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.8261 / SU ML: 0.69 / σ(F): 1.35 / Phase error: 24.13 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2421 1383 5.04 %
Rwork0.1992 26060 -
obs0.2014 27443 98.04 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 37.574 Å2 / ksol: 0.331 e/Å3
Displacement parametersBiso max: 114.72 Å2 / Biso mean: 44.6602 Å2 / Biso min: 18.21 Å2
Baniso -1Baniso -2Baniso -3
1-0.9458 Å20 Å2-0 Å2
2--2.2268 Å2-0 Å2
3----3.1726 Å2
Refinement stepCycle: LAST / Resolution: 2.309→44.28 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4092 0 13 277 4382
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0074209
X-RAY DIFFRACTIONf_angle_d1.0165680
X-RAY DIFFRACTIONf_dihedral_angle_d18.2021567
X-RAY DIFFRACTIONf_chiral_restr0.073584
X-RAY DIFFRACTIONf_plane_restr0.008731
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3088-2.39130.32351180.26192196X-RAY DIFFRACTION84
2.3913-2.48710.2921330.23072524X-RAY DIFFRACTION97
2.4871-2.60020.2441400.22262609X-RAY DIFFRACTION100
2.6002-2.73730.23751340.21992620X-RAY DIFFRACTION100
2.7373-2.90880.27761380.21622629X-RAY DIFFRACTION100
2.9088-3.13330.29251290.22212669X-RAY DIFFRACTION100
3.1333-3.44850.2351550.20462636X-RAY DIFFRACTION100
3.4485-3.94730.24891500.18642647X-RAY DIFFRACTION100
3.9473-4.97210.19491470.15652699X-RAY DIFFRACTION100
4.9721-44.2880.22141390.19172831X-RAY DIFFRACTION100

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