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- PDB-2q3g: Structure of the PDZ domain of human PDLIM7 bound to a C-terminal... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2q3g | ||||||
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Title | Structure of the PDZ domain of human PDLIM7 bound to a C-terminal extension from human beta-tropomyosin | ||||||
![]() | PDZ and LIM domain protein 7 | ||||||
![]() | STRUCTURAL GENOMICS / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() muscle structure development / muscle alpha-actinin binding / filamentous actin / RET signaling / stress fiber / ruffle / ossification / receptor-mediated endocytosis / adherens junction / Z disc ...muscle structure development / muscle alpha-actinin binding / filamentous actin / RET signaling / stress fiber / ruffle / ossification / receptor-mediated endocytosis / adherens junction / Z disc / actin cytoskeleton / actin binding / heart development / actin cytoskeleton organization / cell differentiation / focal adhesion / nucleoplasm / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gileadi, C. / Papagrigoriou, E. / Elkins, J. / Burgess-Brown, N. / Salah, E. / Gileadi, O. / Umeano, C. / Bunkoczi, G. / von Delft, F. / Uppenberg, J. ...Gileadi, C. / Papagrigoriou, E. / Elkins, J. / Burgess-Brown, N. / Salah, E. / Gileadi, O. / Umeano, C. / Bunkoczi, G. / von Delft, F. / Uppenberg, J. / Pike, A.C.W. / Arrowsmith, C.H. / Edwards, A. / Weigelt, J. / Sundstrom, M. / Doyle, D.A. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Unusual binding interactions in PDZ domain crystal structures help explain binding mechanisms Authors: Elkins, J.M. / Gileadi, C. / Shrestha, L. / Phillips, C. / Wang, J. / Muniz, J.R. / Doyle, D.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 92.9 KB | Display | ![]() |
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PDB format | ![]() | 70.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.8 KB | Display | ![]() |
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Full document | ![]() | 452.2 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 18.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2pa1C ![]() 2pktC ![]() 2pntC ![]() 2uzcC ![]() 2v1wC ![]() 2w7rC C: citing same article ( |
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Similar 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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Unit cell |
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Details | the two molecules found in the asu represent two biological units |
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Components
#1: Protein | Mass: 9302.571 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() Strain (production host): BL21(DE3) with with pRARE plasmid encoding rare codon tRNAs,(chloramphenicol-resistant) References: UniProt: Q9NR12 #2: Chemical | #3: Chemical | ChemComp-CL / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37.38 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 0.1M HEPES; 10% isopropanol; 20% PEG 4K, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 11, 2007 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9182 Å / Relative weight: 1 |
Reflection | Resolution: 1.11→39.84 Å / Num. all: 58681 / Num. obs: 58329 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Rmerge(I) obs: 0.042 / Rsym value: 0.038 |
Reflection shell | Resolution: 1.11→1.15 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.144 / Mean I/σ(I) obs: 11 / Rsym value: 0.121 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: homoly based model Resolution: 1.11→39.84 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.97 / SU B: 0.657 / SU ML: 0.015 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / ESU R: 0.031 / ESU R Free: 0.031 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 7.247 Å2
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Refinement step | Cycle: LAST / Resolution: 1.11→39.84 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.11→1.138 Å / Total num. of bins used: 20
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