+Open data
-Basic information
Entry | Database: PDB / ID: 4zb4 | ||||||
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Title | Spliceosome component | ||||||
Components | Pre-mRNA-processing factor 19 | ||||||
Keywords | SPLICING / Spliceosome / ligase | ||||||
Function / homology | Function and homology information generation of catalytic spliceosome for first transesterification step / U2-type catalytic step 1 spliceosome / Prp19 complex / Dual incision in TC-NER / protein K63-linked ubiquitination / Gap-filling DNA repair synthesis and ligation in TC-NER / RING-type E3 ubiquitin transferase / mRNA splicing, via spliceosome / ubiquitin-protein transferase activity / ubiquitin protein ligase activity ...generation of catalytic spliceosome for first transesterification step / U2-type catalytic step 1 spliceosome / Prp19 complex / Dual incision in TC-NER / protein K63-linked ubiquitination / Gap-filling DNA repair synthesis and ligation in TC-NER / RING-type E3 ubiquitin transferase / mRNA splicing, via spliceosome / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / DNA repair / mitochondrion / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Saccharomyces cerevisiae (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Rocha de Moura, T. / Pena, P. | ||||||
Citation | Journal: To Be Published Title: Spliceosome component Authors: Rocha de Moura, T. / Pena, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4zb4.cif.gz | 286 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4zb4.ent.gz | 233.5 KB | Display | PDB format |
PDBx/mmJSON format | 4zb4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zb/4zb4 ftp://data.pdbj.org/pub/pdb/validation_reports/zb/4zb4 | HTTPS FTP |
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-Related structure data
Related structure data | 3lrvS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 40688.684 Da / Num. of mol.: 2 / Fragment: UNP residues 144-503 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast) Strain: S288c / Gene: PRP19, PSO4, YLL036C / Plasmid: pETM11 / Production host: Escherichia coli BL21(DE3) (bacteria) References: UniProt: P32523, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases) #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.1 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 7 / Details: PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
Detector | Type: PSI PILATUS 6M / Detector: PIXEL / Date: May 11, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→50 Å / Num. all: 32176 / Num. obs: 31956 / % possible obs: 99.3 % / Redundancy: 8.2 % / Net I/σ(I): 12.35 |
Reflection shell | Resolution: 2.331→2.396 Å / Rmerge(I) obs: 0.49 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3LRV Resolution: 2.3→48.992 Å / FOM work R set: 0.8041 / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 26.52 / 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 max: 240.05 Å2 / Biso mean: 48.04 Å2 / Biso min: 19.01 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.3→48.992 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12
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