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Open data
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Basic information
Entry | Database: PDB / ID: 4c92 | ||||||
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Title | Crystal structure of the yeast Lsm1-7 complex | ||||||
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![]() | TRANSCRIPTION / LSM1-7 / DECAPPING ACTIVATORS / MRNA DEGRADATION | ||||||
Function / homology | ![]() mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / U6 snRNP / deadenylation-dependent decapping of nuclear-transcribed mRNA / U4/U6 snRNP / P-body assembly / sno(s)RNA-containing ribonucleoprotein complex / spliceosomal tri-snRNP complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / tRNA processing ...mRNA decay by 5' to 3' exoribonuclease / Lsm1-7-Pat1 complex / U6 snRNP / deadenylation-dependent decapping of nuclear-transcribed mRNA / U4/U6 snRNP / P-body assembly / sno(s)RNA-containing ribonucleoprotein complex / spliceosomal tri-snRNP complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / tRNA processing / U2-type prespliceosome / precatalytic spliceosome / nuclear-transcribed mRNA catabolic process / U6 snRNA binding / spliceosomal snRNP assembly / cellular response to glucose starvation / U4/U6 x U5 tri-snRNP complex / catalytic step 2 spliceosome / maturation of SSU-rRNA / spliceosomal complex / P-body / mRNA splicing, via spliceosome / mRNA processing / rRNA processing / ribonucleoprotein complex / chromatin binding / mRNA binding / nucleolus / RNA binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sharif, H. / Conti, E. | ||||||
![]() | ![]() Title: Architecture of the Lsm1-7-Pat1 Complex: A Conserved Assembly in Eukaryotic Mrna Turnover Authors: Sharif, H. / Conti, E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET 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 | ![]() | 138.1 KB | Display | ![]() |
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PDB format | ![]() | 105.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4c8qC ![]() 2y9a ![]() 3bw1S ![]() 4emkS 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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Unit cell |
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Components
-U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN ... , 6 types, 6 molecules BCDEFG
#2: Protein | Mass: 12216.880 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-95 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#3: Protein | Mass: 10039.262 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-89 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#4: Protein | Mass: 13035.543 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-114 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#5: Protein | Mass: 10432.954 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-93 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#6: Protein | Mass: 9406.579 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-86 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
#7: Protein | Mass: 13027.045 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-115 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
-Protein / Non-polymers , 2 types, 109 molecules A![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#1: Protein | Mass: 17287.596 Da / Num. of mol.: 1 / Fragment: RESIDUES 27-172 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#8: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.37 Å3/Da / Density % sol: 48.14 % / Description: MOLECULAR REPLACEMENT WITH CHIMERIC MODEL |
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Crystal grow | Details: 100 MM MES PH 6.0, 40% MPD |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Aug 23, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.998 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→95.57 Å / Num. obs: 62699 / % possible obs: 99.3 % / Observed criterion σ(I): 2 / Redundancy: 2.1 % / Biso Wilson estimate: 46.13 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.3→2.42 Å / Redundancy: 2 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 3.1 / % possible all: 96.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRIES 2Y9A, 3BW1, 4EMK Resolution: 2.299→53.993 Å / SU ML: 0.39 / σ(F): 1.04 / Phase error: 32.36 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.19 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.299→53.993 Å
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Refine LS restraints |
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LS refinement shell |
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