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Open data
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Basic information
Entry | Database: PDB / ID: 1rzx | ||||||
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Title | Crystal Structure of a Par-6 PDZ-peptide Complex | ||||||
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![]() | CELL CYCLE | ||||||
Function / homology | ![]() RAC1 GTPase cycle / RHOV GTPase cycle / terminal branching, open tracheal system / subapical complex / establishment or maintenance of neuroblast polarity / branching involved in open tracheal system development / zonula adherens assembly / RHOU GTPase cycle / establishment of neuroblast polarity / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) ...RAC1 GTPase cycle / RHOV GTPase cycle / terminal branching, open tracheal system / subapical complex / establishment or maintenance of neuroblast polarity / branching involved in open tracheal system development / zonula adherens assembly / RHOU GTPase cycle / establishment of neuroblast polarity / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Asymmetric localization of PCP proteins / establishment or maintenance of polarity of embryonic epithelium / muscle cell postsynaptic specialization / regulation of cellular localization / border follicle cell migration / asymmetric neuroblast division / morphogenesis of a polarized epithelium / apical cortex / apical protein localization / positive regulation of smoothened signaling pathway / establishment or maintenance of epithelial cell apical/basal polarity / centrosome cycle / positive regulation of filopodium assembly / protein kinase inhibitor activity / bicellular tight junction / positive regulation of lamellipodium assembly / synapse assembly / terminal bouton / cell cortex / apical plasma membrane / nucleus / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Peterson, F.C. / Penkert, R.R. / Volkman, F.B. / Prehoda, K.E. | ||||||
![]() | ![]() Title: Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Authors: Peterson, F.C. / Penkert, R.R. / Volkman, B.F. / Prehoda, K.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 31.8 KB | Display | ![]() |
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PDB format | ![]() | 21.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 426.3 KB | Display | ![]() |
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Full document | ![]() | 428.2 KB | Display | |
Data in XML | ![]() | 6.8 KB | Display | |
Data in CIF | ![]() | 8.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ry4C ![]() 1nf3S S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 10497.011 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 700.844 Da / Num. of mol.: 1 / Source method: obtained synthetically Details: This protein was chemically synthesized. The N-terminal has been acetylated (ACE)VKESLV. |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.85 % | ||||||||||||||||||||||||
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Crystal grow | Temperature: 288 K / Method: vapor diffusion, hanging drop / pH: 7.1 Details: 26% PEG6000, 100 mM HEPES, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 288K | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 16 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. all: 7402 / Num. obs: 7357 / % possible obs: 99.4 % |
Reflection shell | Resolution: 2.1→2.18 Å / % possible all: 96 |
Reflection | *PLUS Rmerge(I) obs: 0.036 |
Reflection shell | *PLUS % possible obs: 96.1 % / Num. unique obs: 693 / Rmerge(I) obs: 0.122 / Mean I/σ(I) obs: 10.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1nf3 Resolution: 2.1→30 Å
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Refinement step | Cycle: LAST / Resolution: 2.1→30 Å
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Refinement | *PLUS Rfactor Rfree: 0.26 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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