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Yorodumi- PDB-1hgx: HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE) -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hgx | ||||||
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Title | HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE) | ||||||
Components | HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE | ||||||
Keywords | TRANSFERASE (GLYCOSYLTRANSFERASE) / TRANSFERASE / GLYCOSYLTRANSFERASE / PURINE SALVAGE | ||||||
Function / homology | Function and homology information xanthine phosphoribosyltransferase / XMP salvage / xanthine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase / GMP salvage / guanine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase activity / IMP salvage / nucleotide binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Tritrichomonas foetus (eukaryote) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Somoza, J.R. / Wang, C.C. / Fletterick, R.J. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Crystal structure of the hypoxanthine-guanine-xanthine phosphoribosyltransferase from the protozoan parasite Tritrichomonas foetus. Authors: Somoza, J.R. / Chin, M.S. / Focia, P.J. / Wang, C.C. / Fletterick, R.J. #1: Journal: Mol.Biochem.Parasitol. / Year: 1994 Title: Isolation, Sequencing and Expression of the Gene Encoding Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase of Tritrichomonas Foetus Authors: Chin, M.S. / Wang, C.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hgx.cif.gz | 80.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hgx.ent.gz | 60.5 KB | Display | PDB format |
PDBx/mmJSON format | 1hgx.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hg/1hgx ftp://data.pdbj.org/pub/pdb/validation_reports/hg/1hgx | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 21114.301 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Tritrichomonas foetus (eukaryote) / Strain: KV1 / Plasmid: PBACE / Production host: Escherichia coli (E. coli) References: UniProt: P51900, hypoxanthine phosphoribosyltransferase #2: Chemical | ChemComp-5GP / | #3: Chemical | ChemComp-SO4 / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.62 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 22 ℃ / Method: vapor diffusion, sitting drop / PH range low: 6.8 / PH range high: 6.3 | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: Aug 16, 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 27314 / % possible obs: 91.2 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.063 |
Reflection | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 9999 Å / Num. measured all: 97259 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 1.96 Å / % possible obs: 55.6 % / Rmerge(I) obs: 0.38 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: HUMAN HGPRTASE Resolution: 1.9→6 Å / σ(F): -3 Details: THE TEMPERATURE FACTORS FOR THE FOLLOWING RESIDUES ARE HIGH, AND THE PLACEMENT OF THESE RESIDUES SHOULD BE VIEWED WITH SKEPTICISM: GLU A179 MET B 7 CYS B 71
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Xplor file |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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