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- PDB-1xz8: Pyrr, The Regulator Of The Pyrimidine Biosynthetic Operon In Baci... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1xz8 | ||||||
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Title | Pyrr, The Regulator Of The Pyrimidine Biosynthetic Operon In Bacillus caldolyticus, Nucleotide-bound form | ||||||
![]() | PyrR bifunctional protein | ||||||
![]() | TRANSCRIPTION / TRANSFERASE / TRANSCRIPTION REGULATION / ATTENUATION PROTEIN / RNA-BINDING / PYRIMIDINE BIOSYNTHESIS / PRTASE / URACIL PHOSPHORIBOSYLTRANSFERASE | ||||||
Function / homology | ![]() uracil phosphoribosyltransferase / uracil phosphoribosyltransferase activity / DNA-templated transcription termination / RNA binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Chander, P. / Halbig, K.M. / Miller, J.K. / Fields, C.J. / Bonner, H.K. / Grabner, G.K. / Switzer, R.L. / Smith, J.L. | ||||||
![]() | ![]() Title: Structure of the Nucleotide Complex of PyrR, the pyr Attenuation Protein from Bacillus caldolyticus, Suggests Dual Regulation by Pyrimidine and Purine Nucleotides. Authors: Chander, P. / Halbig, K.M. / Miller, J.K. / Fields, C.J. / Bonner, H.K. / Grabner, G.K. / Switzer, R.L. / Smith, J.L. | ||||||
History |
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Remark 300 | BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S) ...BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 2 CHAIN(S). THE AUTHORS ARE NOT SURE ABOUT WHAT THE BIOLOGICAL MOLECULE FOR THE PROTEIN IS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 80.2 KB | Display | ![]() |
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PDB format | ![]() | 59.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.4 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 16.5 KB | Display | |
Data in CIF | ![]() | 21.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1nonSC ![]() 1xznC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 19967.051 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P41007, uracil phosphoribosyltransferase |
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-Non-polymers , 5 types, 60 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/5GP.gif)
![](data/chem/img/3GP.gif)
![](data/chem/img/U5P.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/5GP.gif)
![](data/chem/img/3GP.gif)
![](data/chem/img/U5P.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | ChemComp-5GP / | #4: Chemical | ChemComp-3GP / | #5: Chemical | ChemComp-U5P / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.53 Å3/Da / Density % sol: 31.7 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: 50mM Na cacodylate,40mM MgCl2,5-6% MPD, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.8→50 Å / Num. obs: 10213 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1NON Resolution: 2.8→50 Å / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.8→50 Å
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Refine LS restraints |
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