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- PDB-1n55: 0.83A resolution structure of the E65Q mutant of Leishmania mexic... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1n55 | ||||||
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Title | 0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate | ||||||
![]() | triosephosphate isomerase![]() | ||||||
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Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kursula, I. / Wierenga, R.K. | ||||||
![]() | ![]() Title: Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution Authors: Kursula, I. / Wierenga, R.K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 140.9 KB | Display | ![]() |
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PDB format | ![]() | 109.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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 on special symmetry positions |
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Components
#1: Protein | ![]() Mass: 27208.236 Da / Num. of mol.: 1 / Mutation: E65Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-PGA / | ||||
#3: Chemical | ![]() #4: Chemical | ![]() #5: Water | ChemComp-HOH / | ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.09 % | ||||||||||||||||||
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Crystal grow![]() | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 4.5 Details: 20% PEG 6000, 0.1 M Na-acetate/NaOH, pH 4.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K | ||||||||||||||||||
Crystal grow | *PLUS Details: Kursula, I., (2001) Eur. J. Biochem., 268, 5189. | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Details: Bent mirror |
Radiation | Monochromator: Triangular / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 0.83→25 Å / Num. all: 243382 / Num. obs: 241678 / % possible obs: 99.3 % / Redundancy: 4.3 % / Biso Wilson estimate: 6.88 Å2 / Rmerge(I) obs: 0.029 / Net I/σ(I): 34 |
Reflection shell | Resolution: 0.83→0.84 Å / Rmerge(I) obs: 0.394 / Mean I/σ(I) obs: 3 / % possible all: 97.2 |
Reflection | *PLUS Lowest resolution: 25 Å |
Reflection shell | *PLUS % possible obs: 97.2 % / Num. unique obs: 11796 |
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Processing
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Refinement | Method to determine structure![]() ![]()
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Refinement step | Cycle: LAST / Resolution: 0.83→25 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELXL / Version: 97 / Classification: refinement | ||||||||||||||||||
Refinement | *PLUS Lowest resolution: 25 Å / Rfactor obs: 0.1026 | ||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||
Refine LS restraints | *PLUS Type: s_plane_restr / Dev ideal: 0.441 |