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- PDB-1s2u: Crystal structure of the D58A phosphoenolpyruvate mutase mutant p... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1s2u | ||||||
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Title | Crystal structure of the D58A phosphoenolpyruvate mutase mutant protein | ||||||
![]() | Phosphoenolpyruvate phosphomutase | ||||||
![]() | ISOMERASE / phosphoenolpyruvate mutase / PEP mutase / phosphonopyruvate / phosphonate biosynthesis pathway | ||||||
Function / homology | ![]() phosphoenolpyruvate mutase / phosphoenolpyruvate mutase activity / organic phosphonate biosynthetic process / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liu, S. / Lu, Z. / Han, Y. / Jia, Y. / Howard, A. / Dunaway-Mariano, D. / Herzberg, O. | ||||||
![]() | ![]() Title: Conformational Flexibility of PEP Mutase Authors: Liu, S. / Lu, Z. / Han, Y. / Jia, Y. / Howard, A. / Dunaway-Mariano, D. / Herzberg, O. | ||||||
History |
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Remark 999 | SEQUENCE THE AUTHORS INFORMED THAT THEIR SEQUENCE IS CORRECT AT THE POSITIONS WHERE IT CONFLICTS ...SEQUENCE THE AUTHORS INFORMED THAT THEIR SEQUENCE IS CORRECT AT THE POSITIONS WHERE IT CONFLICTS WITH THE SWISS PROT SEQUENCE. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 136.5 KB | Display | ![]() |
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PDB format | ![]() | 105.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 455.9 KB | Display | ![]() |
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Full document | ![]() | 464.2 KB | Display | |
Data in XML | ![]() | 29.5 KB | Display | |
Data in CIF | ![]() | 44.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1s2tC ![]() 1s2vC ![]() 1s2wC ![]() 1pymS 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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Details | biological assembly is a tetramer which can be generated from the dimer by the operation: -x+1, y, -z+1/2 |
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Components
#1: Protein | Mass: 32910.336 Da / Num. of mol.: 2 / Mutation: D58A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.6 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: PEG 4000, Glycerol, HEPES, MgCl2, pH 7.0-8.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Monochromator: Si(111) double-crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. obs: 36902 / % possible obs: 94.1 % / Observed criterion σ(I): 1 / Redundancy: 5.48 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 10.4 |
Reflection shell | Resolution: 2→2.05 Å / Rmerge(I) obs: 0.299 / % possible all: 84.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 1pym Resolution: 2→27.7 Å / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2→27.7 Å
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Refine LS restraints |
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