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Yorodumi- PDB-2i6i: crystal structures of the archaeal sulfolobus PTP-fold phosphatase -
+Open data
-Basic information
Entry | Database: PDB / ID: 2i6i | ||||||
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Title | crystal structures of the archaeal sulfolobus PTP-fold phosphatase | ||||||
Components | Sulfolobus solfataricus protein tyrosine phosphatase | ||||||
Keywords | HYDROLASE / PTP domain | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Sulfolobus solfataricus (archaea) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.15 Å | ||||||
Authors | Chu, H.M. / Wang, A.H.J. | ||||||
Citation | Journal: Proteins / Year: 2006 Title: Enzyme-substrate interactions revealed by the crystal structures of the archaeal Sulfolobus PTP-fold phosphatase and its phosphopeptide complexes Authors: Chu, H.M. / Wang, A.H.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2i6i.cif.gz | 43.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2i6i.ent.gz | 30.6 KB | Display | PDB format |
PDBx/mmJSON format | 2i6i.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/i6/2i6i ftp://data.pdbj.org/pub/pdb/validation_reports/i6/2i6i | HTTPS FTP |
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-Related 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: 18433.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Sulfolobus solfataricus (archaea) / Plasmid: pET21 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q97VZ7 |
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#2: 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: 2.34 Å3/Da / Density % sol: 47.37 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 0.1M citrate(pH5.5), 20% PEG3000, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Mar 1, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→50 Å / Num. all: 8891 / Num. obs: 7981 / % possible obs: 89.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.061 / Rsym value: 0.046 / Net I/σ(I): 18.8 |
Reflection shell | Resolution: 2.15→2.23 Å / Redundancy: 2 % / Rmerge(I) obs: 0.199 / Mean I/σ(I) obs: 3.9 / Num. unique all: 735 / Rsym value: 0.183 / % possible all: 77.9 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.15→50 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.15→50 Å
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Refine LS restraints |
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