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- PDB-4up0: Ternary crystal structure of the Pygo2 PHD finger in complex with... -
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Basic information
Entry | Database: PDB / ID: 4up0 | ||||||
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Title | Ternary crystal structure of the Pygo2 PHD finger in complex with the B9L HD1 domain and a H3K4me2 peptide | ||||||
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![]() | TRANSCRIPTION / WNT SIGNALLING / PHD FINGER / BCL9L / HD1 DOMAIN | ||||||
Function / homology | ![]() histone acetyltransferase regulator activity / spermatid nucleus differentiation / regulation of mammary gland epithelial cell proliferation / beta-catenin-TCF complex / mammary gland development / regulation of cell morphogenesis / myoblast differentiation / lens development in camera-type eye / roof of mouth development / skeletal muscle cell differentiation ...histone acetyltransferase regulator activity / spermatid nucleus differentiation / regulation of mammary gland epithelial cell proliferation / beta-catenin-TCF complex / mammary gland development / regulation of cell morphogenesis / myoblast differentiation / lens development in camera-type eye / roof of mouth development / skeletal muscle cell differentiation / somatic stem cell population maintenance / developmental growth / canonical Wnt signaling pathway / Chromatin modifying enzymes / positive regulation of epithelial to mesenchymal transition / telomere organization / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / epigenetic regulation of gene expression / Assembly of the ORC complex at the origin of replication / DNA methylation / Condensation of Prophase Chromosomes / SIRT1 negatively regulates rRNA expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / PRC2 methylates histones and DNA / kidney development / Defective pyroptosis / Deactivation of the beta-catenin transactivating complex / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / negative regulation of transforming growth factor beta receptor signaling pathway / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / brain development / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / HDMs demethylate histones / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / fibrillar center / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / beta-catenin binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / nucleosome / nucleosome assembly / chromatin organization / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / gene expression / HATs acetylate histones / histone binding / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / transcription by RNA polymerase II / transcription coactivator activity / cadherin binding / protein heterodimerization activity / Amyloid fiber formation / chromatin binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Miller, T.C.R. / Fiedler, M. / Rutherford, T.J. / Birchall, K. / Chugh, J. / Bienz, M. | ||||||
![]() | ![]() Title: Competitive Binding of a Benzimidazole to the Histone-Binding Pocket of the Pygo Phd Finger. Authors: Miller, T.C.R. / Rutherford, T.J. / Birchall, K. / Chugh, J. / Fiedler, M. / Bienz, M. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 54.5 KB | Display | ![]() |
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PDB format | ![]() | 38.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4up5C ![]() 2xb1S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 10537.676 Da / Num. of mol.: 1 / Fragment: PHD FINGER, HD1,RESIDUES 327-387,235-263 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Protein/peptide | Mass: 1633.872 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-16 / Source method: obtained synthetically / Details: DIMETHYLATED LYSINE 4 - K4ME2 / Source: (synth.) ![]() | ||||
#3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | GLYCINE (REMNANT OF TEV CLEAVAGE SITE), PYGO2 PHD FINGER ( AAS 327-387), ARTIFICIAL LINKER (8AA ...GLYCINE (REMNANT OF TEV CLEAVAGE SITE), PYGO2 PHD FINGER ( AAS 327-387), ARTIFICIAL | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.1 % / Description: NONE |
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Crystal grow | Details: 1 M SODIUM CITRATE, 0.1 M TRIS PH 7, 0.2 M NACL |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 29, 2011 / Details: MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.976219 Å / Relative weight: 1 |
Reflection | Resolution: 1.28→39.47 Å / Num. obs: 22695 / % possible obs: 99.9 % / Observed criterion σ(I): 2.4 / Redundancy: 11.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 13 |
Reflection shell | Resolution: 1.28→1.3 Å / Redundancy: 12.3 % / Mean I/σ(I) obs: 2.4 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XB1 Resolution: 1.28→39.47 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.971 / SU B: 1.222 / SU ML: 0.024 / Cross valid method: THROUGHOUT / ESU R: 0.042 / ESU R Free: 0.041 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.CHAIN A RESIDUES 383-387 AND 8AA GSGSGSGS LINKER ARE DISORDERED CHAIN A RESIDUE 1263 IS DISORDERED. CHAIN F RESIDUES 7-15 ARE DISORDERED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 21.159 Å2
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Refinement step | Cycle: LAST / Resolution: 1.28→39.47 Å
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Refine LS restraints |
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