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Open data
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Basic information
Entry | Database: PDB / ID: 1ft3 | ||||||
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Title | CRYSTAL STRUCTURE OF TRUNCATED RHOGDI K141A MUTANT | ||||||
![]() | RHO GDP-DISSOCIATION INHIBITOR 1 | ||||||
![]() | SIGNALING PROTEIN INHIBITOR / immunoglobulin fold / beta sandwich motif / isoprenyl-binding domain / GDP-dissociation inhibitor of Rho GTPases | ||||||
Function / homology | ![]() Rho GDP-dissociation inhibitor activity / regulation of synaptic vesicle cycle / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of Rho protein signal transduction / RHOC GTPase cycle / CDC42 GTPase cycle / RHOH GTPase cycle / semaphorin-plexin signaling pathway / Rho protein signal transduction ...Rho GDP-dissociation inhibitor activity / regulation of synaptic vesicle cycle / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of Rho protein signal transduction / RHOC GTPase cycle / CDC42 GTPase cycle / RHOH GTPase cycle / semaphorin-plexin signaling pathway / Rho protein signal transduction / immunological synapse / RHOG GTPase cycle / RHOA GTPase cycle / RAC2 GTPase cycle / RAC1 GTPase cycle / GTPase activator activity / Schaffer collateral - CA1 synapse / regulation of protein localization / cytoskeleton / negative regulation of apoptotic process / extracellular exosome / membrane / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Longenecker, K.L. / Garrard, S.M. / Sheffield, P.J. / Derewenda, Z.S. | ||||||
![]() | ![]() Title: Protein crystallization by rational mutagenesis of surface residues: Lys to Ala mutations promote crystallization of RhoGDI. Authors: Longenecker, K.L. / Garrard, S.M. / Sheffield, P.J. / Derewenda, Z.S. #1: ![]() Title: A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm Authors: Keep, N.H. / Barnes, M. / Barsukov, I. / Badii, R. / Lian, L. / Segal, A.W. / Moody, P.C. / Roberts, G.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 64.9 KB | Display | ![]() |
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PDB format | ![]() | 49.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.5 KB | Display | ![]() |
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Full document | ![]() | 442.5 KB | Display | |
Data in XML | ![]() | 12.7 KB | Display | |
Data in CIF | ![]() | 16.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 |
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4 | ![]()
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Unit cell |
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Details | The asymmetric unit has two monomers. The biologically active species is one monomer. |
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Components
#1: Protein | Mass: 15911.137 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN / Mutation: K141A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.18 Å3/Da / Density % sol: 70.6 % | |||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: ammonium sulfate, Na/K tartrate, sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Dec 6, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9091 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. all: 13249 / Num. obs: 13249 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.3 % / Biso Wilson estimate: 80 Å2 / Rmerge(I) obs: 0.094 / Net I/σ(I): 11 |
Reflection shell | Resolution: 2.8→2.85 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.67 / Num. unique all: 689 / % possible all: 87 |
Reflection | *PLUS Num. measured all: 57299 |
Reflection shell | *PLUS % possible obs: 87 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 1.9 |
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Processing
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Refinement | Resolution: 2.8→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh and Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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