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Yorodumi- PDB-1i8g: SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHO... -
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-Basic information
Entry | Database: PDB / ID: 1i8g | ||||||
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Title | SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25 PHOSPHOTHREONINE PEPTIDE | ||||||
Components |
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Keywords | HYDROLASE/ISOMERASE / CELL DIVISION / NUCLEAR PROTEIN / HYDROLASE-ISOMERASE COMPLEX | ||||||
Function / homology | Function and homology information positive regulation of cell cycle G2/M phase transition / cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division ...positive regulation of cell cycle G2/M phase transition / cis-trans isomerase activity / phosphothreonine residue binding / negative regulation of cell motility / ubiquitin ligase activator activity / regulation of protein localization to nucleus / GTPase activating protein binding / postsynaptic cytosol / mitogen-activated protein kinase kinase binding / regulation of mitotic nuclear division / negative regulation of SMAD protein signal transduction / PI5P Regulates TP53 Acetylation / negative regulation of amyloid-beta formation / cytoskeletal motor activity / phosphoserine residue binding / RHO GTPases Activate NADPH Oxidases / protein peptidyl-prolyl isomerization / positive regulation of protein dephosphorylation / protein-tyrosine-phosphatase / ciliary basal body / positive regulation of GTPase activity / regulation of cytokinesis / negative regulation of protein binding / peptidylprolyl isomerase / protein tyrosine phosphatase activity / peptidyl-prolyl cis-trans isomerase activity / Negative regulators of DDX58/IFIH1 signaling / phosphoprotein binding / synapse organization / negative regulation of transforming growth factor beta receptor signaling pathway / regulation of protein phosphorylation / regulation of protein stability / tau protein binding / neuron differentiation / negative regulation of protein catabolic process / negative regulation of ERK1 and ERK2 cascade / ISG15 antiviral mechanism / beta-catenin binding / positive regulation of canonical Wnt signaling pathway / positive regulation of protein binding / midbody / regulation of gene expression / Regulation of TP53 Activity through Phosphorylation / protein stabilization / response to hypoxia / nuclear speck / positive regulation of protein phosphorylation / cell cycle / cell division / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
Authors | Wintjens, R. / Wieruszeski, J.-M. / Drobecq, H. / Lippens, G. / Landrieu, I. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2001 Title: 1H NMR study on the binding of Pin1 Trp-Trp domain with phosphothreonine peptides. Authors: Wintjens, R. / Wieruszeski, J.M. / Drobecq, H. / Rousselot-Pailley, P. / Buee, L. / Lippens, G. / Landrieu, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1i8g.cif.gz | 158.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1i8g.ent.gz | 137 KB | Display | PDB format |
PDBx/mmJSON format | 1i8g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1i8g_validation.pdf.gz | 366.8 KB | Display | wwPDB validaton report |
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Full document | 1i8g_full_validation.pdf.gz | 460.2 KB | Display | |
Data in XML | 1i8g_validation.xml.gz | 11.8 KB | Display | |
Data in CIF | 1i8g_validation.cif.gz | 18.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i8/1i8g ftp://data.pdbj.org/pub/pdb/validation_reports/i8/1i8g | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 1192.209 Da / Num. of mol.: 1 / Fragment: RESIDUES 63-72 / Source method: obtained synthetically Details: The ligand phosphopeptide was synthesized from Rink amide resin using the Fmoc strategy and activation by HBTU and HOBT in a 431A peptide synthesizer. The sequence of the peptide is ...Details: The ligand phosphopeptide was synthesized from Rink amide resin using the Fmoc strategy and activation by HBTU and HOBT in a 431A peptide synthesizer. The sequence of the peptide is naturally found in Xenopus laevis (African clawed frog). References: UniProt: P30311, protein-tyrosine-phosphatase |
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#2: Protein/peptide | Mass: 4462.899 Da / Num. of mol.: 1 / Fragment: WW DOMAIN (RESIDUES 6-44) / Source method: obtained synthetically Details: The Pin1 WW domain was obtained by peptide synthesis using the BOC-benzyl strategy and the HBTU in situ activation protocol on an Applied 430A peptide synthesizer. The sequence of the ...Details: The Pin1 WW domain was obtained by peptide synthesis using the BOC-benzyl strategy and the HBTU in situ activation protocol on an Applied 430A peptide synthesizer. The sequence of the peptide is naturally found in Homo sapiens (Human). References: UniProt: Q13526, peptidylprolyl isomerase |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Type: 2D NOESY |
-Sample preparation
Details | Contents: sample of 1mM WW domain / 4.5 mM Cdc25 ligand buffer of 50 mM deutered Tris-D2O, pH 6.4, 100 mM NaCl Solvent system: 90% H2O/10% D2O |
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Sample conditions | Ionic strength: 100 mM NaCl / pH: 6.4 / Pressure: ambient / Temperature: 285 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 Details: hybrid of distance geometry / simulated annealing protocol Minimization procedure using CVFF as force field | ||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 10 |