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Yorodumi- PDB-2csw: Solution structure of the FHA domain of human ubiquitin ligase pr... -
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-Basic information
Entry | Database: PDB / ID: 2csw | ||||||
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Title | Solution structure of the FHA domain of human ubiquitin ligase protein RNF8 | ||||||
Components | Ubiquitin ligase protein RNF8 | ||||||
Keywords | LIGASE / 11-stranded beta sandwich / RING finger protein 8 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information sperm DNA condensation / isotype switching / DNA repair-dependent chromatin remodeling / response to ionizing radiation / negative regulation of transcription elongation by RNA polymerase II / protein K63-linked ubiquitination / protein K48-linked ubiquitination / protein autoubiquitination / interstrand cross-link repair / ubiquitin ligase complex ...sperm DNA condensation / isotype switching / DNA repair-dependent chromatin remodeling / response to ionizing radiation / negative regulation of transcription elongation by RNA polymerase II / protein K63-linked ubiquitination / protein K48-linked ubiquitination / protein autoubiquitination / interstrand cross-link repair / ubiquitin ligase complex / epigenetic regulation of gene expression / signal transduction in response to DNA damage / positive regulation of DNA repair / ubiquitin binding / Nonhomologous End-Joining (NHEJ) / RING-type E3 ubiquitin transferase / G2/M DNA damage checkpoint / double-strand break repair via nonhomologous end joining / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / double-strand break repair / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / site of double-strand break / Processing of DNA double-strand break ends / midbody / histone binding / ubiquitin-dependent protein catabolic process / chromosome, telomeric region / cell cycle / cell division / DNA damage response / chromatin binding / ubiquitin protein ligase binding / protein homodimerization activity / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Hayashi, F. / Nagashima, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the FHA domain of human ubiquitin ligase protein RNF8 Authors: Hayashi, F. / Nagashima, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2csw.cif.gz | 851.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2csw.ent.gz | 741.2 KB | Display | PDB format |
PDBx/mmJSON format | 2csw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cs/2csw ftp://data.pdbj.org/pub/pdb/validation_reports/cs/2csw | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16056.050 Da / Num. of mol.: 1 / Fragment: FHA domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: RNF8 / Plasmid: P040322-86 References: UniProt: O76064, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
-Sample preparation
Details | Contents: 1.1mM 13C,15N-labeled protein; 20mM d-TrisHCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3 Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function, structures with the lowest energy, structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |