+Open data
-Basic information
Entry | Database: PDB / ID: 3ik8 | ||||||
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Title | Structure-Based Design of Novel PIN1 Inhibitors (I) | ||||||
Components | Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 | ||||||
Keywords | ISOMERASE / SBDD / PPIase / Cell cycle / Nucleus / Phosphoprotein / Rotamase | ||||||
Function / homology | Function and homology information 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 ...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 / RHO GTPases Activate NADPH Oxidases / phosphoserine residue binding / protein peptidyl-prolyl isomerization / positive regulation of protein dephosphorylation / ciliary basal body / regulation of cytokinesis / negative regulation of protein binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / Negative regulators of DDX58/IFIH1 signaling / phosphoprotein binding / synapse organization / regulation of protein phosphorylation / negative regulation of transforming growth factor beta receptor signaling pathway / 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 GTPase activity / 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 / glutamatergic synapse / positive regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Matthews, D. / Greasley, S. / Ferre, R.A. / Parge, H. | ||||||
Citation | Journal: Bioorg.Med.Chem.Lett. / Year: 2009 Title: Structure-based design of novel human Pin1 inhibitors (I). Authors: Guo, C. / Hou, X. / Dong, L. / Dagostino, E. / Greasley, S. / Ferre, R. / Marakovits, J. / Johnson, M.C. / Matthews, D. / Mroczkowski, B. / Parge, H. / Vanarsdale, T. / Popoff, I. / Piraino, ...Authors: Guo, C. / Hou, X. / Dong, L. / Dagostino, E. / Greasley, S. / Ferre, R. / Marakovits, J. / Johnson, M.C. / Matthews, D. / Mroczkowski, B. / Parge, H. / Vanarsdale, T. / Popoff, I. / Piraino, J. / Margosiak, S. / Thomson, J. / Los, G. / Murray, B.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3ik8.cif.gz | 79.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3ik8.ent.gz | 59.9 KB | Display | PDB format |
PDBx/mmJSON format | 3ik8.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ik/3ik8 ftp://data.pdbj.org/pub/pdb/validation_reports/ik/3ik8 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 13662.197 Da / Num. of mol.: 2 / Fragment: UNP residues 45-163, PIN1 PPIASE DOMAIN / Mutation: K77Q,K82Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PIN1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q13526, peptidylprolyl isomerase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.94 Å3/Da / Density % sol: 36.46 % |
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Crystal grow | Temperature: 286 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.2M ammonium sulfate, 0.9M Na Citrate, 5mM TCEP, 100mM HEPES, , pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 286K |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Nov 20, 2000 / Details: mirrors |
Radiation | Monochromator: Osmic mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→10 Å / Num. all: 16979 / Num. obs: 16979 / % possible obs: 94.4 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Redundancy: 4.6 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 25.7 |
Reflection shell | Resolution: 1.85→1.92 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.169 / Mean I/σ(I) obs: 7.9 / % possible all: 85.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.85→5 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.85→5 Å
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LS refinement shell | Resolution: 1.85→1.93 Å /
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