[English] 日本語
![](img/lk-miru.gif)
- PDB-1qc6: EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1qc6 | ||||||
---|---|---|---|---|---|---|---|
Title | EVH1 domain from ENA/VASP-like protein in complex with ACTA peptide | ||||||
![]() |
| ||||||
![]() | STRUCTURAL PROTEIN / AN INCOMPLETE SEVEN STRANDED ANTI-PARALLEL BETA BARREL CLOSED BY AN ALPHA HELIX / EVH1 DOMAIN / ACTIN-BASED CELL MOTILITY / INTERACTION MODULE | ||||||
Function / homology | ![]() Signaling by ROBO receptors / negative regulation of ruffle assembly / actin nucleation / negative regulation of epithelial cell migration / RHO GTPases Activate Formins / actin filament-based movement / profilin binding / barbed-end actin filament capping / actin polymerization or depolymerization / positive regulation of actin filament polymerization ...Signaling by ROBO receptors / negative regulation of ruffle assembly / actin nucleation / negative regulation of epithelial cell migration / RHO GTPases Activate Formins / actin filament-based movement / profilin binding / barbed-end actin filament capping / actin polymerization or depolymerization / positive regulation of actin filament polymerization / positive regulation of stress fiber assembly / phagocytic vesicle / axon guidance / platelet activation / cellular response to type II interferon / SH3 domain binding / lamellipodium / actin binding / protein homotetramerization / cytoskeleton / focal adhesion / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fedorov, A.A. / Fedorov, E.V. / Gertler, F.B. / Almo, S.C. | ||||||
![]() | ![]() Title: Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function Authors: Fedorov, A.A. / Fedorov, E. / Gertler, F. / Almo, S.C. #1: ![]() Title: Mena, a relative of VASP and Drosophila Enabled is implicated in the control of microfilament dynamics Authors: Gertler, F.B. / Niebuhr, K. / Reinhard, M. / Wehland, J. / Soriano, P. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 55.5 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 43.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 399.7 KB | Display | |
Data in XML | ![]() | 7.5 KB | Display | |
Data in CIF | ![]() | 11.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||
Unit cell |
| ||||||||||
Details | The biological assembly is constructed from chains 1A and 2A / The biological assembly is constructed from chains 1B and 2B |
-
Components
#1: Protein | Mass: 14796.967 Da / Num. of mol.: 2 / Fragment: N-TERMINAL DOMAIN / Mutation: MET 1,14,105,112 MODIFIED TO SELENOMET Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Protein/peptide | Mass: 1304.355 Da / Num. of mol.: 2 / Source method: obtained synthetically Details: THE PROLINE-RICH PEPTIDE PREPARED BY PEPTIDE SYNTHESIS #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.02 Å3/Da / Density % sol: 38 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6 Details: ammonium sulfate, DTT, sodium azide, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K Temp details: room temperature | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||
Detector | Type: ADSC / Detector: CCD / Date: Feb 15, 1999 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
| ||||||||||||
Reflection | Resolution: 2.6→20 Å / Num. all: 8216 / Num. obs: 7926 / % possible obs: 96.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.4 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 18.3 | ||||||||||||
Reflection shell | Resolution: 2.6→2.69 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.298 / Mean I/σ(I) obs: 4.8 / Num. unique all: 723 / % possible all: 88.1 | ||||||||||||
Reflection | *PLUS Rmerge(I) obs: 0.09 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]()
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
Refine LS restraints NCS | NCS model details: RESTRAINTS | |||||||||||||||||||||||||
Xplor file | Serial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: TOPHCSDX.PRO | |||||||||||||||||||||||||
Software | *PLUS Name: ![]() | |||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 8 Å / σ(F): 2 / % reflection Rfree: 8 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
|