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Yorodumi- PDB-1pjz: Solution structure of thiopurine methyltransferase from Pseudomon... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1pjz | ||||||
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Title | Solution structure of thiopurine methyltransferase from Pseudomonas syringae | ||||||
Components | Thiopurine S-methyltransferase | ||||||
Keywords | TRANSFERASE / methyltransferase / polymorphism / S-adenosylmethionine / drug metabolism | ||||||
Function / homology | Function and homology information thiopurine S-methyltransferase / thiopurine S-methyltransferase activity / response to tellurium ion / response to metal ion / methylation / cytoplasm Similarity search - Function | ||||||
Biological species | Pseudomonas syringae pv. pisi (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Authors | Scheuermann, T.H. / Lolis, E. / Hodsdon, M.E. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2003 Title: Tertiary structure of thiopurine methyltransferase from Pseudomonas syringae, a bacterial orthologue of a polymorphic, drug-metabolizing enzyme Authors: Scheuermann, T.H. / Lolis, E. / Hodsdon, M.E. | ||||||
History |
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Remark 999 | SEQUENCE 17 N-terminal residues were deleted from the sequence. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1pjz.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1pjz.ent.gz | 1003.1 KB | Display | PDB format |
PDBx/mmJSON format | 1pjz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1pjz_validation.pdf.gz | 343.9 KB | Display | wwPDB validaton report |
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Full document | 1pjz_full_validation.pdf.gz | 689 KB | Display | |
Data in XML | 1pjz_validation.xml.gz | 150.9 KB | Display | |
Data in CIF | 1pjz_validation.cif.gz | 194.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pj/1pjz ftp://data.pdbj.org/pub/pdb/validation_reports/pj/1pjz | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 22590.494 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas syringae pv. pisi (bacteria) Species: Pseudomonas syringae / Strain: pv. pisi / Gene: TPM / Plasmid: pGEX-2T / Production host: Escherichia coli (E. coli) / Strain (production host): (DE3)BL21 / References: UniProt: O86262, thiopurine S-methyltransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 20 mM Potassium Phosphate, 150 mM NaCl, 0.05% NaN3, 1 uM lupeptin, 1 uM pepstatin, 1 uM PMSF, 1.5 mM protein, uniform (random) labeling with 13C, 15N at known labeling Solvent system: 95% H2O/5% D2O |
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Sample conditions | Ionic strength: 150 mM NaCL / pH: 6.8 / Pressure: 1 atm / Temperature: 293 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
-Processing
NMR software |
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Refinement | Method: simulated annealing, molecular dynamics / Software ordinal: 1 Details: 5000 MD steps at high temp, 35000 steps (cooling), 10000 conjugate gradient minimzation steps | ||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 20 / Conformers submitted total number: 20 |