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Yorodumi- PDB-1d2m: UVRB PROTEIN OF THERMUS THERMOPHILUS HB8; A NUCLEOTIDE EXCISION R... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1d2m | ||||||
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Title | UVRB PROTEIN OF THERMUS THERMOPHILUS HB8; A NUCLEOTIDE EXCISION REPAIR ENZYME | ||||||
Components | EXCINUCLEASE ABC SUBUNIT B | ||||||
Keywords | HYDROLASE / MULTIDOMAIN PROTEIN / RIKEN Structural Genomics/Proteomics Initiative / RSGI / Structural Genomics | ||||||
Function / homology | Function and homology information excinuclease ABC activity / excinuclease repair complex / SOS response / nucleotide-excision repair / ATP hydrolysis activity / DNA binding / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.9 Å | ||||||
Authors | Nakagawa, N. / Sugahara, M. / Masui, R. / Kato, R. / Fukuyama, K. / Kuramitsu, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: J.Biochem.(Tokyo) / Year: 1999 Title: Crystal structure of Thermus thermophilus HB8 UvrB protein, a key enzyme of nucleotide excision repair. Authors: Nakagawa, N. / Sugahara, M. / Masui, R. / Kato, R. / Fukuyama, K. / Kuramitsu, S. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Crystallization and Preliminary X-ray Diffraction Studies of a DNA Excision Repair Enzyme, UvrB, from Thermus thermophilus HB8 Authors: Shibata, A. / Nakagawa, N. / Sugahara, M. / Masui, R. / Kato, R. / Kuramitsu, S. / Fukuyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1d2m.cif.gz | 131.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1d2m.ent.gz | 101.8 KB | Display | PDB format |
PDBx/mmJSON format | 1d2m.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/d2/1d2m ftp://data.pdbj.org/pub/pdb/validation_reports/d2/1d2m | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 76266.117 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB8 / Plasmid: PET11A / Production host: Escherichia coli (E. coli) / References: UniProt: Q56243 | ||||
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#2: Sugar | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.68 Å3/Da / Density % sol: 66.6 % | |||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.1 Details: lithium sulfate, B-octylgulucoside, glycerol, MES, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K | |||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Details: Shibata, A., (1999) Acta Crystallogr.D55, 704. | |||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.708 |
Detector | Type: RIGAKU RAXIS / Detector: IMAGE PLATE / Date: Jun 20, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.708 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→30 Å / Num. obs: 82751 / % possible obs: 93.5 % / Observed criterion σ(I): 1 / Redundancy: 4 % / Biso Wilson estimate: 15.7 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 21.5 |
Reflection shell | Resolution: 1.9→1.96 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.166 / Num. unique all: 3377 / % possible all: 76 |
Reflection | *PLUS Lowest resolution: 30 Å |
-Processing
Software |
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Refinement | Resolution: 1.9→30 Å / σ(F): 1 / Stereochemistry target values: ENGH & HUBER
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Refinement step | Cycle: LAST / Resolution: 1.9→30 Å
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Software | *PLUS Name: CNS / Classification: refinement | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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