+
Open data
-
Basic information
Entry | Database: PDB / ID: 1tx4 | ||||||
---|---|---|---|---|---|---|---|
Title | RHO/RHOGAP/GDP(DOT)ALF4 COMPLEX | ||||||
![]() |
| ||||||
![]() | COMPLEX(GTPASE ACTIVATN/PROTO-ONCOGENE) / COMPLEX (GTPASE ACTIVATION-PROTO-ONCOGENE) / ![]() ![]() | ||||||
Function / homology | ![]() negative regulation of endocytic recycling / transferrin transport / aortic valve formation / alpha-beta T cell lineage commitment / mitotic cleavage furrow formation / bone trabecula morphogenesis / positive regulation of lipase activity / endothelial tube lumen extension / skeletal muscle satellite cell migration / positive regulation of vascular associated smooth muscle contraction ...negative regulation of endocytic recycling / transferrin transport / aortic valve formation / alpha-beta T cell lineage commitment / mitotic cleavage furrow formation / bone trabecula morphogenesis / positive regulation of lipase activity / endothelial tube lumen extension / skeletal muscle satellite cell migration / positive regulation of vascular associated smooth muscle contraction / angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure / SLIT2:ROBO1 increases RHOA activity / RHO GTPases Activate Rhotekin and Rhophilins / Roundabout signaling pathway / negative regulation of intracellular steroid hormone receptor signaling pathway / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of neural precursor cell proliferation / cleavage furrow formation / regulation of modification of postsynaptic actin cytoskeleton / regulation of osteoblast proliferation / forebrain radial glial cell differentiation / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rittinger, K. / Walker, P.A. / Smerdon, S.J. / Gamblin, S.J. | ||||||
![]() | ![]() Title: Structure at 1.65 A of RhoA and its GTPase-activating protein in complex with a transition-state analogue. Authors: Rittinger, K. / Walker, P.A. / Eccleston, J.F. / Smerdon, S.J. / Gamblin, S.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 102.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 74.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1am4S S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
-Protein , 2 types, 2 molecules AB
#1: Protein | Mass: 22586.848 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
---|---|
#2: Protein | ![]() Mass: 20032.906 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
-Non-polymers , 4 types, 500 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/ALF.gif)
![](data/chem/img/GDP.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/ALF.gif)
![](data/chem/img/GDP.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | ChemComp-MG / |
---|---|
#4: Chemical | ChemComp-ALF / |
#5: Chemical | ChemComp-GDP / ![]() |
#6: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.56 Å3/Da / Density % sol: 45 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | pH: 6 Details: PROTEIN WAS CRYSTALLIZED FROM 18% PEG 2000 MME 100MM MES PH6.0 10MM MGCL2, 3MM DTT, 3MM NAN3, 114MM AMMONIUM SULFATE 400UM PROTEIN COMPLEX WITH 1MM ALCL3 AND 10MM NAF. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLAGE / Date: Jun 1, 1997 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.65→6 Å / Num. obs: 42992 / % possible obs: 80.5 % / Redundancy: 3.7 % / Rmerge(I) obs: 0.065 / Net I/σ(I): 16.1 |
Reflection shell | Resolution: 1.65→1.72 Å / % possible all: 60.8 |
Reflection | *PLUS Num. measured all: 160124 |
Reflection shell | *PLUS % possible obs: 60.8 % / Rmerge(I) obs: 0.324 / Mean I/σ(I) obs: 2.3 |
-
Processing
Software |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure![]() ![]() Starting model: 1AM4 Resolution: 1.65→6 Å
| ||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→6 Å
| ||||||||||||||||
Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.169 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
|