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- PDB-1hgx: HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE) -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hgx | ||||||
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Title | HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE (HGXPRTASE) | ||||||
![]() | HYPOXANTHINE-GUANINE-XANTHINE PHOSPHORIBOSYLTRANSFERASE | ||||||
![]() | TRANSFERASE (GLYCOSYLTRANSFERASE) / TRANSFERASE / GLYCOSYLTRANSFERASE / PURINE SALVAGE | ||||||
Function / homology | ![]() xanthine phosphoribosyltransferase / XMP salvage / xanthine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase / guanine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase activity / GMP salvage / IMP salvage / nucleotide binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Somoza, J.R. / Wang, C.C. / Fletterick, R.J. | ||||||
![]() | ![]() 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: ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.8 KB | Display | ![]() |
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PDB format | ![]() | 60.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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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.) ![]() ![]() ![]() 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: ![]() |
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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 |
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Processing
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Refinement | Method to determine structure: ![]() 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: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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