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- PDB-1btn: STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A PH DOMAIN -
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Open data
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Basic information
Entry | Database: PDB / ID: 1btn | ||||||
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Title | STRUCTURE OF THE BINDING SITE FOR INOSITOL PHOSPHATES IN A PH DOMAIN | ||||||
![]() | BETA-SPECTRIN | ||||||
![]() | SIGNAL TRANSDUCTION PROTEIN | ||||||
Function / homology | ![]() Interaction between L1 and Ankyrins / regulation of SMAD protein signal transduction / RHOV GTPase cycle / membrane assembly / RHOU GTPase cycle / NCAM signaling for neurite out-growth / central nervous system formation / cuticular plate / spectrin / COPI-mediated anterograde transport ...Interaction between L1 and Ankyrins / regulation of SMAD protein signal transduction / RHOV GTPase cycle / membrane assembly / RHOU GTPase cycle / NCAM signaling for neurite out-growth / central nervous system formation / cuticular plate / spectrin / COPI-mediated anterograde transport / RAF/MAP kinase cascade / plasma membrane organization / Golgi to plasma membrane protein transport / actin filament capping / M band / ankyrin binding / cortical actin cytoskeleton / cortical cytoskeleton / mitotic cytokinesis / axolemma / endomembrane system / positive regulation of interleukin-2 production / central nervous system development / protein localization to plasma membrane / cell projection / positive regulation of protein localization to plasma membrane / structural constituent of cytoskeleton / phospholipid binding / actin filament binding / cell junction / GTPase binding / actin cytoskeleton organization / postsynapse / postsynaptic density / calmodulin binding / glutamatergic synapse / protein-containing complex binding / nucleolus / protein-containing complex / membrane / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Wilmanns, M. / Hyvoenen, M. / Saraste, M. | ||||||
![]() | ![]() Title: Structure of the binding site for inositol phosphates in a PH domain. Authors: Hyvonen, M. / Macias, M.J. / Nilges, M. / Oschkinat, H. / Saraste, M. / Wilmanns, M. #1: ![]() Title: Structure of the Ph Domain from Beta-Spectrin Authors: Macias, M.J. / Musacchio, A. / Postingl, H. / Nilges, M. / Saraste, M. / Oschkinat, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 37.1 KB | Display | ![]() |
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PDB format | ![]() | 23.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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
#1: Protein | Mass: 12287.853 Da / Num. of mol.: 1 / Fragment: PH DOMAIN, RESIDUES 2199 - 2304 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-I3P / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 50 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 6.5 / Details: pH 6.5 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Wavelength: 1.54 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 1, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2→1000 Å / Num. obs: 7830 / % possible obs: 89.6 % / Observed criterion σ(I): 0 / Redundancy: 5.4 % / Rmerge(I) obs: 0.047 |
Reflection | *PLUS Num. measured all: 41713 / Rmerge(I) obs: 0.047 |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 1
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Displacement parameters | Biso mean: 27.9 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.27 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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