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- PDB-1u27: Triglycine variant of the ARNO Pleckstrin Homology Domain in comp... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1u27 | ||||||
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Title | Triglycine variant of the ARNO Pleckstrin Homology Domain in complex with Ins(1,3,4,5)P4 | ||||||
![]() | Cytohesin 2 | ||||||
![]() | LIPID BINDING PROTEIN / Pleckstrin Homology domain / lipid binding / phosphoinositide | ||||||
Function / homology | ![]() extrinsic component of postsynaptic specialization membrane / Intra-Golgi traffic / negative regulation of dendrite development / inositol 1,4,5 trisphosphate binding / regulation of ARF protein signal transduction / bicellular tight junction / regulation of cell adhesion / ruffle / guanyl-nucleotide exchange factor activity / adherens junction ...extrinsic component of postsynaptic specialization membrane / Intra-Golgi traffic / negative regulation of dendrite development / inositol 1,4,5 trisphosphate binding / regulation of ARF protein signal transduction / bicellular tight junction / regulation of cell adhesion / ruffle / guanyl-nucleotide exchange factor activity / adherens junction / growth cone / postsynapse / lipid binding / glutamatergic synapse / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Cronin, T.C. / DiNitto, J.P. / Czech, M.P. / Lambright, D.G. | ||||||
![]() | ![]() Title: Structural determinants of phosphoinositide selectivity in splice variants of Grp1 family PH domains Authors: Cronin, T.C. / DiNitto, J.P. / Czech, M.P. / Lambright, D.G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 39.3 KB | Display | ![]() |
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PDB format | ![]() | 26.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1u29C ![]() 1u2bC ![]() 1fgyS 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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Unit cell |
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Components
#1: Protein | Mass: 15054.076 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-4IP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47.1 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 4000, sodium MES, 10% glycerol, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jul 1, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→20 Å / Num. all: 5810 / Num. obs: 5810 / % possible obs: 88.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 |
Reflection shell | Resolution: 2.3→2.37 Å / % possible all: 99.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1FGY Resolution: 2.3→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: Residues 377 and 388, and several atoms for residues 286, 298, 318, 331 and 336 were modeled into this structure with zero occupancy because they are part of the PH domain and were not deleted or mutated.
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Solvent computation | Bsol: 35.3169 Å2 / ksol: 0.306501 e/Å3 | ||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.3→20 Å
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Refine LS restraints |
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Xplor file |
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