+Open data
-Basic information
Entry | Database: PDB / ID: 1m36 | ||||||
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Title | Solution Structure of a CCHC Zinc Finger from MOZ | ||||||
Components | Monocytic leukemia zinc finger protein | ||||||
Keywords | DNA BINDING PROTEIN / zinc finger / acetyl transferase | ||||||
Function / homology | Function and homology information histone H4K5 acetyltransferase activity / histone H4K8 acetyltransferase activity / histone H3K14 acetyltransferase activity / histone H4K12 acetyltransferase activity / histone H4K16 acetyltransferase activity / myeloid cell differentiation / regulation of developmental process / MOZ/MORF histone acetyltransferase complex / regulation of hemopoiesis / protein acetylation ...histone H4K5 acetyltransferase activity / histone H4K8 acetyltransferase activity / histone H3K14 acetyltransferase activity / histone H4K12 acetyltransferase activity / histone H4K16 acetyltransferase activity / myeloid cell differentiation / regulation of developmental process / MOZ/MORF histone acetyltransferase complex / regulation of hemopoiesis / protein acetylation / acetyltransferase activity / chromosome organization / histone acetyltransferase activity / histone acetyltransferase / Regulation of TP53 Activity through Acetylation / regulation of signal transduction by p53 class mediator / transcription coregulator activity / PML body / nucleosome assembly / nucleosome / cellular senescence / HATs acetylate histones / DNA-binding transcription factor binding / transcription coactivator activity / nuclear speck / negative regulation of DNA-templated transcription / positive regulation of gene expression / nucleolus / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics torsion angle dynamics | ||||||
Authors | Kwan, A.H.Y. / Gell, D.A. / Liew, C.K. / Mackay, J.P. | ||||||
Citation | Journal: To be Published Title: Solution Structure of a CCHC Zinc Finger from MOZ Authors: Kwan, A.H.Y. / Gell, D.A. / Liew, C.K. / Mackay, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1m36.cif.gz | 225.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1m36.ent.gz | 194.7 KB | Display | PDB format |
PDBx/mmJSON format | 1m36.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/1m36 ftp://data.pdbj.org/pub/pdb/validation_reports/m3/1m36 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 4045.970 Da / Num. of mol.: 1 / Fragment: residues 3-33 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MOZ / Plasmid: pGEX-2T / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q92794 |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D NMR homonuclear techniques |
-Sample preparation
Details | Contents: 0.5mM MOZ protein (533-563), 1mM TCEP, 0.7mM ZnSO4, 95% H2O, 5% D2O Solvent system: 95% H2O/5% D2O |
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Sample conditions | pH: 5.6 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics torsion angle dynamics Software ordinal: 1 Details: Structure calculations were performed using the package ARIA 1.1 (Ambiguous Restraints in Iterative Assignment). Final structures are based on 832 unambiguous NOE-derived distance ...Details: Structure calculations were performed using the package ARIA 1.1 (Ambiguous Restraints in Iterative Assignment). Final structures are based on 832 unambiguous NOE-derived distance constraints, 1 set of ambiguous NOE-derived distance constraints and 19 additional dihedral angle restraints. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 |