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- PDB-1j4p: NMR STRUCTURE OF THE FHA1 DOMAIN OF RAD53 IN COMPLEX WITH A RAD9-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1j4p | ||||||
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Title | NMR STRUCTURE OF THE FHA1 DOMAIN OF RAD53 IN COMPLEX WITH A RAD9-DERIVED PHOSPHOTHREONINE (AT T155) PEPTIDE | ||||||
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![]() | TRANSFERASE/CELL CYCLE / FHA DOMAIN / RAD53 / RAD9 / PHOSPHOTHREONINE / PHOSPHOPROTEIN / TRANSFERASE-CELL CYCLE COMPLEX | ||||||
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 2438 RESTRAINTS. AMONG THEM, 3 ARTIFICAL CONSTRAINTS, 192 TALOS- DERIVED DIHEDRAL ANGLE RESTRAINS, 78 RESTRAINTS FROM H-BOND, 16 INTERMOLECULAR DISTANCE CONSTRAINS, AND 2149 INTRA-FHA1, INTRA- PEPTIDE DISTANCE CONSTRAINTS. | ||||||
![]() | Yuan, C. / Yongkiettrakul, S. / Byeon, I.-J.L. / Zhou, S. / Tsai, M.-D. | ||||||
![]() | ![]() Title: Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53. Authors: Yuan, C. / Yongkiettrakul, S. / Byeon, I.J. / Zhou, S. / Tsai, M.D. #1: ![]() Title: Structure of the Fha1 Domain of Yeast Rad53 and Identification of Binding Sites for Both Fha1 and its Target Protein Rad9. Authors: Liao, H. / Yuan, C. / Su, M.I. / Yongkiettrakul, S. / Qin, D. / Li, H. / Byeon, I.J. / Pei, D. / 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 | ![]() | 71.6 KB | Display | ![]() |
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PDB format | ![]() | 54.2 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 258.2 KB | Display | ![]() |
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Full document | ![]() | 258 KB | Display | |
Data in XML | ![]() | 5.9 KB | Display | |
Data in CIF | ![]() | 7.2 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: 17093.490 Da / Num. of mol.: 1 / Fragment: N-TERMINAL FHA DOMAIN (FHA1) 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: 1617.754 Da / Num. of mol.: 1 / Fragment: RESIDUES 149-161 / Source method: obtained synthetically Details: THIS PHOSPHOTHREONINE 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 FHA1 U-15N,13C 10 MM SODIUM PHOSPHATE BUFFER (PH 6.5), 1MM DTT, AND 1 MM EDTA; 90% H2O, 10% D2O |
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Sample conditions | Ionic strength: 10 mM SODIUM PHOSPHATE, 1mM 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 2438 RESTRAINTS. AMONG THEM, 3 ARTIFICAL CONSTRAINTS, 192 TALOS- DERIVED DIHEDRAL ANGLE RESTRAINS, 78 RESTRAINTS FROM H-BOND, 16 ...Method: THE COMPLEX STRUCTURES ARE GENERATED USING A TOTAL OF 2438 RESTRAINTS. AMONG THEM, 3 ARTIFICAL CONSTRAINTS, 192 TALOS- DERIVED DIHEDRAL ANGLE RESTRAINS, 78 RESTRAINTS FROM H-BOND, 16 INTERMOLECULAR DISTANCE CONSTRAINS, AND 2149 INTRA-FHA1, INTRA- PEPTIDE DISTANCE CONSTRAINTS. Software ordinal: 1 | ||||||||||||
NMR ensemble | Conformers submitted total number: 1 |