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- PDB-1j4l: SOLUTION STRUCTURE OF THE FHA2 DOMAIN OF RAD53 COMPLEXED WITH A P... -
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Basic information
Entry | Database: PDB / ID: 1j4l | ||||||
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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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![]() | TRANSFERASE / FHA DOMAIN / RAD53 / RAD9 / PHOSPHOTHREONINE / PHOSPHOPROTEIN | ||||||
Function / homology | ![]() deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA strand resection involved in replication fork processing / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / dual-specificity kinase / mitotic intra-S DNA damage checkpoint signaling / DNA replication origin binding ...deoxyribonucleoside triphosphate biosynthetic process / negative regulation of DNA strand resection involved in replication fork processing / meiotic recombination checkpoint signaling / telomere maintenance in response to DNA damage / SUMOylation of transcription factors / negative regulation of phosphorylation / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / dual-specificity kinase / mitotic intra-S DNA damage checkpoint signaling / DNA replication origin binding / negative regulation of DNA damage checkpoint / DNA replication initiation / regulation of DNA repair / enzyme activator activity / mitotic G1 DNA damage checkpoint signaling / protein serine/threonine/tyrosine kinase activity / DNA damage checkpoint signaling / nucleotide-excision repair / protein localization / double-strand break repair / histone binding / double-stranded DNA binding / protein tyrosine kinase activity / regulation of cell cycle / protein kinase activity / DNA repair / protein serine kinase activity / protein serine/threonine kinase activity / chromatin / positive regulation of transcription by RNA polymerase II / ATP binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / THE COMPLEX STRUCTURES ARE GENERATED USING A TOTAL OF 3369 RESTRAINTS, 3181 DISTANCE RESTRAINTS, AND 188 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS. | ||||||
![]() | 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 | ![]() | 71.8 KB | Display | ![]() |
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PDB format | ![]() | 53.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 256.8 KB | Display | ![]() |
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Full document | ![]() | 256.6 KB | Display | |
Data in XML | ![]() | 6.3 KB | Display | |
Data in CIF | ![]() | 7.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with an alcohol group as acceptor |
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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: SOLUTION NMR | ||||||||||||||||||||
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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 |
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Sample conditions | Ionic strength: 10 mM SODIUM PHOSPHATE, 1 mM DTT, AND 1 mM EDTA pH: 6.50 / Pressure: AMBIENT / Temperature: 293.00 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 800 MHz |
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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 | Conformers submitted total number: 1 |