+Open data
-Basic information
Entry | Database: PDB / ID: 1z7g | ||||||
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Title | Free human HGPRT | ||||||
Components | Hypoxanthine-guanine phosphoribosyltransferase | ||||||
Keywords | TRANSFERASE / flexibility / trans cis peptide bond isomerization / nucleotide binding | ||||||
Function / homology | Function and homology information adenine metabolic process / Defective HPRT1 disrupts guanine and hypoxanthine salvage / GMP catabolic process / cerebral cortex neuron differentiation / hypoxanthine salvage / positive regulation of dopamine metabolic process / lymphocyte proliferation / hypoxanthine phosphoribosyltransferase / guanine salvage / hypoxanthine metabolic process ...adenine metabolic process / Defective HPRT1 disrupts guanine and hypoxanthine salvage / GMP catabolic process / cerebral cortex neuron differentiation / hypoxanthine salvage / positive regulation of dopamine metabolic process / lymphocyte proliferation / hypoxanthine phosphoribosyltransferase / guanine salvage / hypoxanthine metabolic process / IMP metabolic process / guanine phosphoribosyltransferase activity / hypoxanthine phosphoribosyltransferase activity / grooming behavior / GMP salvage / Purine salvage / IMP salvage / striatum development / AMP salvage / dopaminergic neuron differentiation / purine nucleotide biosynthetic process / purine ribonucleoside salvage / Azathioprine ADME / dendrite morphogenesis / dopamine metabolic process / central nervous system neuron development / response to amphetamine / locomotory behavior / T cell mediated cytotoxicity / protein homotetramerization / nucleotide binding / magnesium ion binding / extracellular exosome / identical protein binding / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Keough, D.T. / Brereton, I.M. / de Jersey, J. / Guddat, L.W. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: The Crystal Structure of Free Human Hypoxanthine-guanine Phosphoribosyltransferase Reveals Extensive Conformational Plasticity Throughout the Catalytic Cycle Authors: Keough, D.T. / Brereton, I.M. / de Jersey, J. / Guddat, L.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1z7g.cif.gz | 176.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1z7g.ent.gz | 139.7 KB | Display | PDB format |
PDBx/mmJSON format | 1z7g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1z7g_validation.pdf.gz | 452.3 KB | Display | wwPDB validaton report |
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Full document | 1z7g_full_validation.pdf.gz | 465.9 KB | Display | |
Data in XML | 1z7g_validation.xml.gz | 35.5 KB | Display | |
Data in CIF | 1z7g_validation.cif.gz | 50.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z7/1z7g ftp://data.pdbj.org/pub/pdb/validation_reports/z7/1z7g | HTTPS FTP |
-Related structure data
Related structure data | 1hmpS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Details | The biological unit is a tetramer. The asymmetric unit consists of two seperate dimers. Tetramers are generated by crystallographic two fold axes of symmetry. |
-Components
#1: Protein | Mass: 24481.217 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HPRT1, HPRT Plasmid details: recombinant plasmid pHTM was obtained by site directed mutagenesis of pRG1 which in turn is derived from pT7-7 Plasmid: pHTM / Production host: Escherichia coli (E. coli) / Strain (production host): S 606 References: UniProt: P00492, hypoxanthine phosphoribosyltransferase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 39.1 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 4.6 Details: 0.2 M ammonium acetate, 0.1 M sodium acetate, 30% PEG4000, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-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: Jun 3, 2003 / Details: Osmic |
Radiation | Monochromator: Single wavelength / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→46.3 Å / Num. all: 66957 / Num. obs: 66957 / % possible obs: 95.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 2.5 % / Rmerge(I) obs: 0.062 / Rsym value: 0.062 / Net I/σ(I): 12.3 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.288 / Mean I/σ(I) obs: 2.2 / Num. unique all: 5419 / Rsym value: 0.288 / % possible all: 79.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1HMP Resolution: 1.9→46.3 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 1 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 59.11 Å2 | |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→46.3 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.97 Å / Rfactor Rfree error: 0.034
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Xplor file |
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