+Open data
-Basic information
Entry | Database: PDB / ID: 2xl3 | ||||||
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Title | WDR5 IN COMPLEX WITH AN RBBP5 PEPTIDE AND HISTONE H3 PEPTIDE | ||||||
Components |
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Keywords | TRANSCRIPTION / MLL COMPLEX / H3K4 METHYLATION / WD-40 BETA-PROPELLER | ||||||
Function / homology | Function and homology information Formation of WDR5-containing histone-modifying complexes / Chromatin modifying enzymes / Interleukin-7 signaling / HDMs demethylate histones / Formation of the beta-catenin:TCF transactivating complex / PRC2 methylates histones and DNA / HATs acetylate histones / PKMTs methylate histone lysines / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / RMTs methylate histone arginines ...Formation of WDR5-containing histone-modifying complexes / Chromatin modifying enzymes / Interleukin-7 signaling / HDMs demethylate histones / Formation of the beta-catenin:TCF transactivating complex / PRC2 methylates histones and DNA / HATs acetylate histones / PKMTs methylate histone lysines / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / RMTs methylate histone arginines / Factors involved in megakaryocyte development and platelet production / Estrogen-dependent gene expression / Neddylation / MLL3/4 complex / Set1C/COMPASS complex / MLL1/2 complex / ATAC complex / NSL complex / histone H3K4 methyltransferase activity / : / histone methyltransferase complex / regulation of tubulin deacetylation / regulation of cell division / MLL1 complex / regulation of embryonic development / histone acetyltransferase complex / positive regulation of gluconeogenesis / transcription initiation-coupled chromatin remodeling / methylated histone binding / skeletal system development / gluconeogenesis / mitotic spindle / structural constituent of chromatin / response to estrogen / neuron projection development / nucleosome / chromatin organization / histone binding / transcription cis-regulatory region binding / regulation of cell cycle / protein heterodimerization activity / DNA damage response / nucleolus / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å | ||||||
Authors | Odho, Z. / Southall, S.M. / Wilson, J.R. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2010 Title: Characterisation of a Novel Wdr5 Binding Site that Recruits Rbbp5 Through a Conserved Motif and Enhances Methylation of H3K4 by Mll1. Authors: Odho, Z. / Southall, S.M. / Wilson, J.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2xl3.cif.gz | 135.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2xl3.ent.gz | 105.1 KB | Display | PDB format |
PDBx/mmJSON format | 2xl3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xl/2xl3 ftp://data.pdbj.org/pub/pdb/validation_reports/xl/2xl3 | HTTPS FTP |
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-Related structure data
Related structure data | 2xl2C 2h13S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper: (Code: given Matrix: (0.998316, -0.000389, 0.058006), Vector: |
-Components
#1: Protein | Mass: 36635.438 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P61965 #2: Protein/peptide | Mass: 1541.524 Da / Num. of mol.: 2 / Fragment: RESIDUES 369-381 / Source method: obtained synthetically / Source: (synth.) MUS MUSCULUS (house mouse) / References: UniProt: Q8BX09 #3: Protein/peptide | Mass: 1097.248 Da / Num. of mol.: 2 / Fragment: AMINO TERMINAL TAIL, RESIDUES 2-9 / Source method: obtained synthetically / Source: (synth.) MUS MUSCULUS (house mouse) / References: UniProt: P68433 #4: Chemical | #5: Water | ChemComp-HOH / | Sequence details | NON NATIVE CARBOXY TERMINAL TYROSINE NON NATIVE TYROSINE AT AMINO TERMINAL | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.45 Å3/Da / Density % sol: 49.7 % / Description: NONE |
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Crystal grow | pH: 8 / Details: 0.2M K2SO4 20 % PEG 3350, pH 8.0 |
-Data collection
Diffraction | Mean temperature: 80 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 |
Detector | Type: ADSC CCD / Detector: CCD / Date: Nov 25, 2009 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→86.3 Å / Num. obs: 16657 / % possible obs: 98.7 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Biso Wilson estimate: 32 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 7.2 |
Reflection shell | Resolution: 2.7→2.9 Å / Redundancy: 3 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.5 / % possible all: 99 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2H13 Resolution: 2.7→41.688 Å / SU ML: 0.3 / σ(F): 0.02 / Phase error: 27.11 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 25.69 Å2 / ksol: 0.323 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.1 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→41.688 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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