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Yorodumi- PDB-1h56: Structural and biochemical characterization of a new magnesium io... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1h56 | ||||||
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Title | Structural and biochemical characterization of a new magnesium ion binding site near Tyr94 in the restriction endonuclease PvuII | ||||||
Components | TYPE II RESTRICTION ENZYME PVUII | ||||||
Keywords | ENDONUCLEASE / TYPE II RESTRICTION ENDONUCLEASE / HYDROLASE / NUCLEASE | ||||||
Function / homology | Function and homology information type II site-specific deoxyribonuclease / type II site-specific deoxyribonuclease activity / DNA restriction-modification system / DNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | PROTEUS VULGARIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3 Å | ||||||
Authors | Spyrida, A. / Matzen, C. / Lanio, T. / Jeltsch, A. / Simoncsits, A. / Athanasiadis, A. / Scheuring-Vanamee, E. / Kokkinidis, M. / Pingoud, A. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Structural and Biochemical Characterization of a New Mg(2+) Binding Site Near Tyr94 in the Restriction Endonuclease PvuII. Authors: Spyridaki, A. / Matzen, C. / Lanio, T. / Jeltsch, A. / Simoncsits, A. / Athanasiadis, A. / Scheuring-Vanamee, E. / Kokkinidis, M. / Pingoud, A. #1: Journal: Nat.Struct.Biol. / Year: 1994 Title: Crystal Structure of PvuII Endonuclease Reveals Extensive Structural Homologies to EcoRV Authors: Athanasiadis, A. / Vlassi, M. / Kotsifaki, D. / Tucker, P.A. / Wilson, K.S. / Kokkinidis, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h56.cif.gz | 77.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1h56.ent.gz | 58.7 KB | Display | PDB format |
PDBx/mmJSON format | 1h56.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h5/1h56 ftp://data.pdbj.org/pub/pdb/validation_reports/h5/1h56 | HTTPS FTP |
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-Related structure data
Related structure data | 1pvuS 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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Unit cell |
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-Components
#1: Protein | Mass: 18239.799 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) PROTEUS VULGARIS (bacteria) / Plasmid: PPVU1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): HB101 References: UniProt: P23657, type II site-specific deoxyribonuclease #2: Chemical | #3: 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: 2.83 Å3/Da / Density % sol: 56.61 % |
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Crystal grow | pH: 5 / Details: pH 5.00 |
Crystal grow | *PLUS Method: other / Details: Athanasiadis, A., (1991) J. Mol. Biol., 222, 451. |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11 / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 15, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 3→8 Å / Num. obs: 8104 / % possible obs: 92.3 % / Redundancy: 1.8 % / Rmerge(I) obs: 0.13 |
Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 8 Å / Rmerge(I) obs: 0.13 |
-Processing
Software |
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Refinement | Method to determine structure: FOURIER SYNTHESIS Starting model: PDB ENTRY 1PVU Resolution: 3→8 Å / Rfactor Rfree error: 0.009 / Cross valid method: THROUGHOUT / σ(F): 0
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 3→8 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3→3.18 Å / Rfactor Rfree error: 0.029 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 3 Å / Lowest resolution: 8 Å / % reflection Rfree: 10 % / Rfactor Rfree: 0.264 / Rfactor Rwork: 0.153 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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