+
Open data
-
Basic information
Entry | Database: PDB / ID: 1ft0 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF TRUNCATED HUMAN RHOGDI K113A 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 / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of synaptic vesicle cycle / regulation of Rho protein signal transduction / RHOC GTPase cycle / CDC42 GTPase cycle / semaphorin-plexin signaling pathway / Rho protein signal transduction / RHOH GTPase cycle ...Rho GDP-dissociation inhibitor activity / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of synaptic vesicle cycle / regulation of Rho protein signal transduction / RHOC GTPase cycle / CDC42 GTPase cycle / semaphorin-plexin signaling pathway / Rho protein signal transduction / RHOH GTPase cycle / 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 |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 65.2 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 49.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 |
| ||||||||
Unit cell |
| ||||||||
Details | The asymmetric unit has two monomers. The biologically active species is one monomer. |
-
Components
#1: Protein | Mass: 15911.137 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN / Mutation: K113A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.1 Å3/Da / Density % sol: 70 % | |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: ammonium sulfate, Na/K tartrate, and sodium citrate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | |||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
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: 2.6→20 Å / Num. all: 15110 / Num. obs: 15110 / % possible obs: 92.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Biso Wilson estimate: 69 Å2 / Rmerge(I) obs: 0.058 / Net I/σ(I): 16.8 |
Reflection shell | Resolution: 2.6→2.66 Å / Redundancy: 4 % / Rmerge(I) obs: 0.333 / Num. unique all: 1015 / % possible all: 94.9 |
Reflection | *PLUS Num. measured all: 73487 |
Reflection shell | *PLUS % possible obs: 94.9 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 2.7 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.6→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh and Huber
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→20 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|