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Yorodumi- PDB-2dhx: Solution Structure of the RRM Domain in the Human Poly (ADP-ribos... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2dhx | ||||||
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Title | Solution Structure of the RRM Domain in the Human Poly (ADP-ribose) Polymerase Family, Member 10 Variant | ||||||
Components | poly (ADP-ribose) polymerase family, member 10 variant | ||||||
Keywords | RNA BINDING PROTEIN / poly (ADP-ribose) polymerase family / RRM domain / RNA-binding / structural genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information negative regulation of protein K63-linked ubiquitination / NAD+- protein-lysine ADP-ribosyltransferase activity / NAD biosynthesis via nicotinamide riboside salvage pathway / Nicotinamide salvaging / Maturation of nucleoprotein / Maturation of nucleoprotein / K63-linked polyubiquitin modification-dependent protein binding / protein auto-ADP-ribosylation / protein poly-ADP-ribosylation / negative regulation of NF-kappaB transcription factor activity ...negative regulation of protein K63-linked ubiquitination / NAD+- protein-lysine ADP-ribosyltransferase activity / NAD biosynthesis via nicotinamide riboside salvage pathway / Nicotinamide salvaging / Maturation of nucleoprotein / Maturation of nucleoprotein / K63-linked polyubiquitin modification-dependent protein binding / protein auto-ADP-ribosylation / protein poly-ADP-ribosylation / negative regulation of NF-kappaB transcription factor activity / NAD+-protein ADP-ribosyltransferase activity / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ ADP-ribosyltransferase activity / translesion synthesis / negative regulation of fibroblast proliferation / nucleotidyltransferase activity / transcription corepressor activity / chromatin organization / DNA-binding transcription factor binding / viral protein processing / negative regulation of gene expression / nucleolus / Golgi apparatus / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, restrained molecular dynamics | ||||||
Authors | Zhao, C. / Kigawa, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution Structure of the RRM Domain in the Human Poly (ADP-ribose) Polymerase Family, Member 10 Variant Authors: Zhao, C. / Kigawa, T. / Tochio, N. / Koshiba, S. / Inoue, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2dhx.cif.gz | 584.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2dhx.ent.gz | 490.5 KB | Display | PDB format |
PDBx/mmJSON format | 2dhx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dh/2dhx ftp://data.pdbj.org/pub/pdb/validation_reports/dh/2dhx | 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: 10714.036 Da / Num. of mol.: 1 / Fragment: RRM domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: PARP10 / Plasmid: P050822-12 / References: GenBank: 62897387, UniProt: Q53GL7*PLUS |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.22mM RRM domain U-15N, 13C; 20mM d-Tris-HCl (pH7.0); 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10%D2O Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 296.0 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, restrained molecular dynamics Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20 |