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- PDB-1k2n: Solution Structure of the FHA2 domain of Rad53 Complexed with a P... -
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Basic information
Entry | Database: PDB / ID: 1k2n | ||||||
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Title | Solution Structure of the FHA2 domain of Rad53 Complexed with a Phosphothreonyl Peptide Derived from Rad9 | ||||||
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Function / homology | ![]() deoxyribonucleoside triphosphate biosynthetic process / G2/M DNA damage checkpoint / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / negative regulation of DNA strand resection involved in replication fork processing / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / meiotic recombination checkpoint signaling / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Byeon, I.-J.L. / Yongkiettrakul, S. / Tsai, M.-D. | ||||||
![]() | ![]() Title: Solution structure of the yeast Rad53 FHA2 complexed with a phosphothreonine peptide pTXXL: comparison with the structures of FHA2-pYXL and FHA1-pTXXD complexes. Authors: Byeon, I.J. / Yongkiettrakul, S. / Tsai, M.D. #1: ![]() Title: II. Structure and Specificity of the Interaction between the FHA2 Domain of Rad53 and Phosphotyrosyl Peptides. Authors: Wang, P. / Byeon, I.J. / Liao, H. / Beebe, K.D. / Yongkiettrakul, S. / Pei, D. / Tsai, M.D. #2: ![]() Title: Structure and Function of a New Phosphopeptide-binding Domain Containing the FHA2 of Rad53. Authors: Liao, H. / Byeon, I.J. / Tsai, M.D. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
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PDB format | ![]() | 907.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 18148.758 Da / Num. of mol.: 1 / Fragment: C-terminal FHA domain (FHA2) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Gene: SPK1 or RAD53 / Plasmid: pGEX-4T / Species (production host): Escherichia coli / Production host: ![]() ![]() ![]() References: UniProt: P22216, ![]() |
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#2: Protein/peptide | ![]() Mass: 1137.130 Da / Num. of mol.: 1 / Fragment: Residues 599-607 / Source method: obtained synthetically Details: This phosphothreonyl peptide was chemically synthesized. References: UniProt: P14737 |
-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. |
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Sample preparation
Details | Contents: 0.5 mM FHA2 U-15N,13C; 1.5 mM phosphothreonyl peptide of Rad9; 10 mM sodium phosphate(pH 6.5), 1 mM DTT, and 1 mM EDTA Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 10 mM sodium phosphate, 1 mM DTT, and 1 mM EDTA pH: 6.5 / Pressure: ambient / Temperature: 293 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![]() |
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Processing
NMR software |
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Refinement | Method: The complex structures are generated using a total of 3369 restraints, 3181 distance restraints, and 188 TALOS-derived dihedral angle restraints. Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |