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Yorodumi- PDB-2b2a: Crystal Structure of the TEN domain of the Telomerase Reverse Tra... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2b2a | ||||||
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Title | Crystal Structure of the TEN domain of the Telomerase Reverse Transcriptase | ||||||
Components | Telomerase reverse transcriptase | ||||||
Keywords | TRANSFERASE / Telomerase / TERT / Reverse Transcriptase / RT | ||||||
Function / homology | Function and homology information telomerase RNA reverse transcriptase activity / telomerase RNA binding / telomerase holoenzyme complex / telomeric DNA binding / telomere maintenance via telomerase / RNA-directed DNA polymerase / chromosome, telomeric region / metal ion binding Similarity search - Function | ||||||
Biological species | Tetrahymena thermophila (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.22 Å | ||||||
Authors | Jacobs, S.A. / Podell, E.R. / Cech, T.R. | ||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2006 Title: Crystal structure of the essential N-terminal domain of telomerase reverse transcriptase. Authors: Jacobs, S.A. / Podell, E.R. / Cech, T.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2b2a.cif.gz | 109.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2b2a.ent.gz | 85.4 KB | Display | PDB format |
PDBx/mmJSON format | 2b2a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b2/2b2a ftp://data.pdbj.org/pub/pdb/validation_reports/b2/2b2a | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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3 |
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Unit cell |
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-Components
#1: Protein | Mass: 23621.818 Da / Num. of mol.: 3 / Fragment: TEN domain / Mutation: L87M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tetrahymena thermophila (eukaryote) / Gene: TERT / Plasmid: pET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: O77448, RNA-directed DNA polymerase #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: 2.1 Å3/Da / Density % sol: 41.8 % |
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Crystal grow | Temperature: 289 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 2000 MMe, Magnesium Nitrate hexahydrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.2.1 / Wavelength: 1.000, 0.953725, 0.97957, 0.97976 | |||||||||||||||
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jun 17, 2005 | |||||||||||||||
Radiation | Monochromator: Double crystal, Si(111) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.22→500 Å / Num. all: 28712 / Num. obs: 28712 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.3 % / Biso Wilson estimate: 18 Å2 / Rmerge(I) obs: 0.109 / Rsym value: 0.109 / Net I/σ(I): 15.5 | |||||||||||||||
Reflection shell | Resolution: 2.22→2.3 Å / Redundancy: 4.55 % / Rmerge(I) obs: 0.622 / Mean I/σ(I) obs: 2.1 / Num. unique all: 2811 / % possible all: 99.4 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.22→19.71 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 123680.98 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 32.0637 Å2 / ksol: 0.345341 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 37.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.22→19.71 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.22→2.36 Å / Rfactor Rfree error: 0.016 / Total num. of bins used: 6
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Xplor file |
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