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Yorodumi- PDB-5x2b: Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP -
+Open data
-Basic information
Entry | Database: PDB / ID: 5x2b | ||||||
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Title | Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP | ||||||
Components | (Sulfotransferase) x 3 | ||||||
Keywords | TRANSFERASE | ||||||
Function / homology | Function and homology information Transferases; Transferring sulfur-containing groups; Sulfotransferases / sulfotransferase activity Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.08 Å | ||||||
Authors | Kanekiyo, M. / Teramoto, T. / Kakuta, Y. | ||||||
Citation | Journal: To Be Published Title: Crystal structure of mouse sulfotransferase SULT7A1 complexed with PAP Authors: Tanaka, S. / Kakuta, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5x2b.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb5x2b.ent.gz | 875.3 KB | Display | PDB format |
PDBx/mmJSON format | 5x2b.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/x2/5x2b ftp://data.pdbj.org/pub/pdb/validation_reports/x2/5x2b | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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Unit cell |
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-Components
-Protein , 3 types, 12 molecules CABEIKLDFGHJ
#1: Protein | Mass: 32664.318 Da / Num. of mol.: 7 / Fragment: UNP residues 7-287 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Sult6b2, Gm766 / Production host: Escherichia coli (E. coli) References: UniProt: B7ZWN4, Transferases; Transferring sulfur-containing groups; Sulfotransferases #2: Protein | | Mass: 32480.127 Da / Num. of mol.: 1 / Fragment: UNP residues 10-287 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Sult6b2, Gm766 / Production host: Escherichia coli (E. coli) References: UniProt: B7ZWN4, Transferases; Transferring sulfur-containing groups; Sulfotransferases #3: Protein | Mass: 32593.240 Da / Num. of mol.: 4 / Fragment: UNP residues 7-287 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Sult6b2, Gm766 / Production host: Escherichia coli (E. coli) References: UniProt: B7ZWN4, Transferases; Transferring sulfur-containing groups; Sulfotransferases |
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-Non-polymers , 4 types, 1713 molecules
#4: Chemical | ChemComp-A3P / #5: Chemical | ChemComp-CA / #6: Chemical | #7: 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: 2.48 Å3/Da / Density % sol: 50.38 % |
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Crystal grow | Temperature: 294.5 K / Method: vapor diffusion, hanging drop / Details: PEG |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 1 Å | |||||||||||||||
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 1, 2011 | |||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||
Reflection twin |
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Reflection | Resolution: 2.08→50 Å / Num. obs: 229447 / % possible obs: 99.8 % / Redundancy: 3.7 % / Rsym value: 0.085 / Net I/σ(I): 16.8 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.08→50 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.95 / Cross valid method: THROUGHOUT / ESU R Free: 0.039 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33.903 Å2
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Refinement step | Cycle: 1 / Resolution: 2.08→50 Å
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Refine LS restraints |
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