+Open data
-Basic information
Entry | Database: PDB / ID: 2ad1 | ||||||
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Title | Human Sulfotransferase SULT1C2 | ||||||
Components | Sulfotransferase 1C2 | ||||||
Keywords | TRANSFERASE / x-ray crystallography / sulfate conjugation / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | Function and homology information aryl sulfotransferase / aryl sulfotransferase activity / Cytosolic sulfonation of small molecules / flavonoid metabolic process / 3'-phosphoadenosine 5'-phosphosulfate metabolic process / ethanol catabolic process / sulfation / sulfotransferase activity / Paracetamol ADME / doxorubicin metabolic process ...aryl sulfotransferase / aryl sulfotransferase activity / Cytosolic sulfonation of small molecules / flavonoid metabolic process / 3'-phosphoadenosine 5'-phosphosulfate metabolic process / ethanol catabolic process / sulfation / sulfotransferase activity / Paracetamol ADME / doxorubicin metabolic process / xenobiotic metabolic process / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Dong, A. / Dombrovski, L. / Loppnau, P. / Edwards, A.M. / Arrowsmith, C.H. / Weigelt, J. / Sundstrom, M. / Bochkarev, A. / Plotnikov, A.N. / Structural Genomics Consortium (SGC) | ||||||
Citation | Journal: Plos Biol. / Year: 2007 Title: Structural and chemical profiling of the human cytosolic sulfotransferases. Authors: Allali-Hassani, A. / Pan, P.W. / Dombrovski, L. / Najmanovich, R. / Tempel, W. / Dong, A. / Loppnau, P. / Martin, F. / Thornton, J. / Thonton, J. / Edwards, A.M. / Bochkarev, A. / Plotnikov, ...Authors: Allali-Hassani, A. / Pan, P.W. / Dombrovski, L. / Najmanovich, R. / Tempel, W. / Dong, A. / Loppnau, P. / Martin, F. / Thornton, J. / Thonton, J. / Edwards, A.M. / Bochkarev, A. / Plotnikov, A.N. / Vedadi, M. / Arrowsmith, C.H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2ad1.cif.gz | 68.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2ad1.ent.gz | 49.3 KB | Display | PDB format |
PDBx/mmJSON format | 2ad1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ad1_validation.pdf.gz | 424.9 KB | Display | wwPDB validaton report |
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Full document | 2ad1_full_validation.pdf.gz | 432.4 KB | Display | |
Data in XML | 2ad1_validation.xml.gz | 13.3 KB | Display | |
Data in CIF | 2ad1_validation.cif.gz | 18.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ad/2ad1 ftp://data.pdbj.org/pub/pdb/validation_reports/ad/2ad1 | HTTPS FTP |
-Related structure data
Related structure data | 1zd1C 2gwhC 2h8kC 1zhe S: Starting model for refinement C: citing same article (ref.) |
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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: 35020.141 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SULT1C2 / Plasmid: pET28 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) References: UniProt: O75897, Transferases; Transferring sulfur-containing groups; Sulfotransferases |
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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: 2.7 Å3/Da / Density % sol: 54.7 % |
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Crystal grow | Temperature: 300 K / Method: vapor diffusion / pH: 4.6 Details: 20%PEG 3350, 0.2M Li citracte pH4.6, VAPOR DIFFUSION, temperature 300K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 29, 2005 / Details: VeriMax |
Radiation | Monochromator: mirror / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 25032 / Num. obs: 25032 / % possible obs: 93.7 % / Observed criterion σ(I): 0 / Redundancy: 10.7 % / Biso Wilson estimate: 37.4 Å2 / Rmerge(I) obs: 0.059 / Rsym value: 0.059 / Net I/σ(I): 14.6 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 9.5 % / Rmerge(I) obs: 0.767 / Mean I/σ(I) obs: 2.89 / Num. unique all: 1881 / Rsym value: 0.767 / % possible all: 72.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1ZHE 1zhe Resolution: 2→50 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.931 / SU B: 4.143 / SU ML: 0.117 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.174 / ESU R Free: 0.166 / 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: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 42.747 Å2
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Refinement step | Cycle: LAST / Resolution: 2→50 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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