+Open data
-Basic information
Entry | Database: PDB / ID: 2hde | ||||||
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Title | Solution Structure of Human SAP18 | ||||||
Components | Histone deacetylase complex subunit SAP18 | ||||||
Keywords | TRANSCRIPTION / HDAC / histone deacetylase / Sin3 / Gli / Bicoid / GAGA / transcriptional repressor | ||||||
Function / homology | Function and homology information ASAP complex / regulation of alternative mRNA splicing, via spliceosome / negative regulation of mRNA splicing, via spliceosome / histone deacetylase complex / RNA splicing / HDACs deacetylate histones / NoRC negatively regulates rRNA expression / mRNA processing / transcription corepressor activity / nuclear body ...ASAP complex / regulation of alternative mRNA splicing, via spliceosome / negative regulation of mRNA splicing, via spliceosome / histone deacetylase complex / RNA splicing / HDACs deacetylate histones / NoRC negatively regulates rRNA expression / mRNA processing / transcription corepressor activity / nuclear body / nuclear speck / positive regulation of apoptotic process / regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Restrained molecular dynamics (Torsion angle, Cartesian dynamics) | ||||||
Authors | McCallum, S.A. / Yin, J.P. / Pan, B. / Fairbrother, W.J. | ||||||
Citation | Journal: Biochemistry / Year: 2006 Title: Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly. Authors: McCallum, S.A. / Bazan, J.F. / Merchant, M. / Yin, J. / Pan, B. / de Sauvage, F.J. / Fairbrother, W.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hde.cif.gz | 919.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hde.ent.gz | 800.5 KB | Display | PDB format |
PDBx/mmJSON format | 2hde.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hd/2hde ftp://data.pdbj.org/pub/pdb/validation_reports/hd/2hde | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16920.244 Da / Num. of mol.: 1 / Fragment: residues 6-149 / Mutation: C26S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SAP18 / Plasmid: pET / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) RIL-codon plus / References: UniProt: O00422 |
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-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 3D triple resonance techniques |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 50mM sodium phosphate, 50mM sodium chloride pH: 5.5 / 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 |
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-Processing
NMR software |
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Refinement | Method: Restrained molecular dynamics (Torsion angle, Cartesian dynamics) Software ordinal: 1 Details: Cyana version 1.06 and Candid version 1.1 were also used for refinement | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |