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Yorodumi- PDB-3u3o: Crystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3u3o | ||||||
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Title | Crystal structure of Human SULT1A1 bound to PAP and two 3-Cyano-7-hydroxycoumarin | ||||||
Components | Sulfotransferase 1A1 | ||||||
Keywords | TRANSFERASE / Arylsulfotransferase / PAP / 3-CYANO-7-HYDROXYCOUMARIN / Xenobiotics | ||||||
Function / homology | Function and homology information aryl sulfotransferase / flavonol 3-sulfotransferase activity / steroid sulfotransferase activity / 3'-phosphoadenosine 5'-phosphosulfate binding / aryl sulfotransferase activity / Cytosolic sulfonation of small molecules / flavonoid metabolic process / 3'-phosphoadenosine 5'-phosphosulfate metabolic process / sulfation / ethanol catabolic process ...aryl sulfotransferase / flavonol 3-sulfotransferase activity / steroid sulfotransferase activity / 3'-phosphoadenosine 5'-phosphosulfate binding / aryl sulfotransferase activity / Cytosolic sulfonation of small molecules / flavonoid metabolic process / 3'-phosphoadenosine 5'-phosphosulfate metabolic process / sulfation / ethanol catabolic process / sulfotransferase activity / catecholamine metabolic process / Paracetamol ADME / amine metabolic process / estrogen metabolic process / xenobiotic metabolic process / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Guttman, C. / Berger, I. / Aharoni, A. / Zarivach, R. | ||||||
Citation | Journal: Plos One / Year: 2011 Title: The molecular basis for the broad substrate specificity of human sulfotransferase 1A1. Authors: Berger, I. / Guttman, C. / Amar, D. / Zarivach, R. / Aharoni, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3u3o.cif.gz | 144.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3u3o.ent.gz | 112.7 KB | Display | PDB format |
PDBx/mmJSON format | 3u3o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/u3/3u3o ftp://data.pdbj.org/pub/pdb/validation_reports/u3/3u3o | 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: 36391.664 Da / Num. of mol.: 1 / Fragment: unp residues 1-295 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Strain: Homo sapiensHuman / Gene: hSULT1A1, OK/SW-cl.88, STP, STP1, SULT1A1 / Plasmid: pET32tr / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P50225, aryl sulfotransferase | ||||||
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#2: Chemical | #3: Chemical | ChemComp-A3P / | #4: Water | ChemComp-HOH / | Sequence details | THESE CONFLICTS ARISE FROM POLYMORPHISM OF THE HSULT1A1 GENE (H213). THE CLOSEST SEQUENCE TO THE ...THESE CONFLICTS ARISE FROM POLYMORPHI | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.46 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 6.5 Details: Magnesium chloride, BIS-TRIS, Polyethylene glycol 3,350, pH 6.5, vapor diffusion, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 20, 2009 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2→62.269 Å / Num. all: 25600 / Num. obs: 25600 / % possible obs: 93.6 % / Redundancy: 4.1 % / Rsym value: 0.108 / Net I/σ(I): 10.3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→62.269 Å / Cor.coef. Fo:Fc: 0.928 / Cor.coef. Fo:Fc free: 0.912 / Occupancy max: 1 / Occupancy min: 0.05 / SU B: 6.716 / SU ML: 0.09 / SU R Cruickshank DPI: 0.1676 / Cross valid method: THROUGHOUT / ESU R: 0.168 / ESU R Free: 0.148 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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 / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.632 Å2
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Refinement step | Cycle: LAST / Resolution: 2→62.269 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.052 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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