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- PDB-4cc3: Complex of human Tuba C-terminal SH3 domain and Mena proline-rich... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4cc3 | ||||||
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Title | Complex of human Tuba C-terminal SH3 domain and Mena proline-rich peptide - H3 | ||||||
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![]() | STRUCTURAL PROTEIN / TUBA / SRC HOMOLOGY 3 / SH3 DOMAIN / MENA / NDPP-1 / PROLINE- RICH PEPTIDE / ACTIN CYTOSKELETON / CORTICAL TENSION | ||||||
Function / homology | ![]() Signaling by ROBO receptors / actin polymerization-dependent cell motility / profilin binding / Golgi stack / actin polymerization or depolymerization / regulation of small GTPase mediated signal transduction / CDC42 GTPase cycle / cilium assembly / stress fiber / guanyl-nucleotide exchange factor activity ...Signaling by ROBO receptors / actin polymerization-dependent cell motility / profilin binding / Golgi stack / actin polymerization or depolymerization / regulation of small GTPase mediated signal transduction / CDC42 GTPase cycle / cilium assembly / stress fiber / guanyl-nucleotide exchange factor activity / filopodium / cellular response to leukemia inhibitory factor / neural tube closure / actin filament organization / axon guidance / SH3 domain binding / cell-cell junction / actin cytoskeleton / presynapse / lamellipodium / actin binding / regulation of cell shape / actin cytoskeleton organization / cytoskeleton / intracellular signal transduction / neuron projection / focal adhesion / synapse / Golgi apparatus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Polle, L. / Rigano, L. / Julian, R. / Ireton, K. / Schubert, W.-D. | ||||||
![]() | ![]() Title: Structural Details of Human Tuba Recruitment by Inlc of Listeria Monocytogenes Elucidate Bacterial Cell-Cell Spreading. Authors: Polle, L. / Rigano, L.A. / Julian, R. / Ireton, K. / Schubert, W. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 137 KB | Display | ![]() |
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PDB format | ![]() | 109.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 719.8 KB | Display | ![]() |
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Full document | ![]() | 723.2 KB | Display | |
Data in XML | ![]() | 14.7 KB | Display | |
Data in CIF | ![]() | 21.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4cc2C ![]() 4cc4C ![]() 4cc7C ![]() 1zuuS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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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Components
#1: Protein | Mass: 7712.617 Da / Num. of mol.: 4 / Fragment: C-TERMINAL SH3 DOMAIN, RESIDUES 1513-1577 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1163.321 Da / Num. of mol.: 4 / Fragment: PROLINE-RICH PEPTIDE, RESIDUES 547-558 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #3: Chemical | #4: Chemical | ChemComp-PE4 / | #5: Water | ChemComp-HOH / | Sequence details | THE FIRST TWO RESIDUES OF THE SEQUENCE GP ARE REMNANTS OF THE FUSION PROTEIN CLEAVAGE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 53 % / Description: NONE |
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Crystal grow | pH: 5.5 / Details: 2.5 M NACL, 0.1 M BIS-TRIS PH 5.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 18, 2011 / Details: KIRKPATRICK-BAEZ PAIR OF BI-MORPH MIRRORS |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
Reflection | Resolution: 1.97→50 Å / Num. obs: 25648 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 4.2 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 16.9 |
Reflection shell | Resolution: 1.97→2.09 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 3 / % possible all: 95.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ZUU Resolution: 1.97→34.33 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.957 / SU B: 5.721 / SU ML: 0.085 / Cross valid method: THROUGHOUT / ESU R: 0.033 / ESU R Free: 0.03 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 47.781 Å2
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Refinement step | Cycle: LAST / Resolution: 1.97→34.33 Å
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Refine LS restraints |
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