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Open data
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Basic information
Entry | Database: PDB / ID: 2xeq | ||||||
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Title | Human PatL1 C-terminal domain | ||||||
![]() | PAT1 HOMOLOG 1, | ||||||
![]() | RNA BINDING PROTEIN / MRNA DECAPPING / P-BODIES | ||||||
Function / homology | ![]() poly(G) binding / mRNA decay by 5' to 3' exoribonuclease / deadenylation-dependent decapping of nuclear-transcribed mRNA / P-body assembly / poly(U) RNA binding / P-body / PML body / cytoplasmic ribonucleoprotein granule / nuclear speck / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Tritschler, F. / Weichenrieder, O. | ||||||
![]() | ![]() Title: The C-Terminal Alpha-Alpha Superhelix of Pat is Required for Mrna Decapping in Metazoa. Authors: Braun, J.E. / Tritschler, F. / Haas, G. / Igreja, C. / Truffault, V. / Weichenrieder, O. / Izaurralde, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 198.7 KB | Display | ![]() |
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PDB format | ![]() | 161.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 460.4 KB | Display | ![]() |
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Full document | ![]() | 484.9 KB | Display | |
Data in XML | ![]() | 36.4 KB | Display | |
Data in CIF | ![]() | 48.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xerC ![]() 2xesSC 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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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 29604.238 Da / Num. of mol.: 4 / Fragment: C-TERMINAL DOMAIN, RESIDUES 517-767 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Sequence details | THE FIRST 5 AMINO ACIDS GPQDP RESULT FROM THE 5' CLONING SITE. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52.4 % / Description: NONE |
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Crystal grow | pH: 7.8 Details: 0.1 M BIS-TRIS-PROPANE, PH 7.8, 10% PEG3350, 0.2 M NA3-CITRATE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 8, 2008 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9794 Å / Relative weight: 1 |
Reflection | Resolution: 3.1→43.9 Å / Num. obs: 22432 / % possible obs: 99.4 % / Observed criterion σ(I): 0 / Redundancy: 4.7 % / Biso Wilson estimate: 70.18 Å2 / Rsym value: 0.13 / Net I/σ(I): 9.1 |
Reflection shell | Resolution: 3.1→3.18 Å / Redundancy: 4.8 % / Mean I/σ(I) obs: 1.9 / Rsym value: 0.88 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XES Resolution: 3.1→43.919 Å / SU ML: 0.47 / σ(F): 1.21 / Phase error: 28.04 / Stereochemistry target values: ML Details: RESIDUES 512-514 AND 573-576 AND 704-711 AND 766-767 OF CHAIN A ARE DISORDERED. RESIDUES 512-514 AND 573-577 AND 703-710 AND 766-767 OF CHAIN B ARE DISORDERED. RESIDUES 512-514 AND 574-577 ...Details: RESIDUES 512-514 AND 573-576 AND 704-711 AND 766-767 OF CHAIN A ARE DISORDERED. RESIDUES 512-514 AND 573-577 AND 703-710 AND 766-767 OF CHAIN B ARE DISORDERED. RESIDUES 512-514 AND 574-577 AND 704-711 AND 766-767 OF CHAIN C ARE DISORDERED. RESIDUES 512-515 AND 663-670 AND 704-710 AND 766-767 OF CHAIN D ARE DISORDERED.
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 44.788 Å2 / ksol: 0.305 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 78 Å2
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Refinement step | Cycle: LAST / Resolution: 3.1→43.919 Å
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Refine LS restraints |
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LS refinement shell |
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