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Open data
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Basic information
Entry | Database: PDB / ID: 5t12 | ||||||
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Title | N-terminal domain of Enzyme 1 - Nitrogen | ||||||
![]() | Phosphoenolpyruvate--protein phosphotransferase | ||||||
![]() | TRANSFERASE / PTSNtr / phosphotransfer | ||||||
Function / homology | ![]() phosphoenolpyruvate-protein phosphotransferase / phosphoenolpyruvate-protein phosphotransferase activity / phosphoenolpyruvate-dependent sugar phosphotransferase system / response to organonitrogen compound / kinase activity / phosphorylation / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Stanley, A.M. / Botos, I. / Buchanan, S.K. | ||||||
![]() | ![]() Title: Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. Authors: Strickland, M. / Stanley, A.M. / Wang, G. / Botos, I. / Schwieters, C.D. / Buchanan, S.K. / Peterkofsky, A. / Tjandra, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 61.8 KB | Display | ![]() |
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PDB format | ![]() | 43.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 424 KB | Display | ![]() |
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Full document | ![]() | 425.1 KB | Display | |
Data in XML | ![]() | 10.7 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5t1nC ![]() 5t1oC ![]() 1zymS 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
#1: Protein | Mass: 28323.018 Da / Num. of mol.: 1 / Fragment: residues 170-424 / Mutation: H356Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: ptsP, AC789_1c31510, ACU90_23270, AML37_15090, AWH59_07225, WQ89_09920 Production host: ![]() ![]() References: UniProt: A0A0E1LBH7, UniProt: P37177*PLUS, phosphoenolpyruvate-protein phosphotransferase | ||
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#2: Chemical | ChemComp-IOD / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.64 Å3/Da / Density % sol: 53.49 % |
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Crystal grow | Temperature: 298.15 K / Method: vapor diffusion, hanging drop Details: 1.0M Potassium/Sodium tartrate 0.1M imidazole 8.0 0.2M NaCl 1.0M sodium iodide |
-Data collection
Diffraction | Mean temperature: 90 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 21, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.299→33.221 Å / Num. obs: 11880 / % possible obs: 96.2 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.112 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2.299→2.38 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.509 / Mean I/σ(I) obs: 1.48 / % possible all: 90.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ZYM Resolution: 2.299→33.221 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 0 / Phase error: 30.31
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.299→33.221 Å
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Refine LS restraints |
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LS refinement shell |
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