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Open data
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Basic information
Entry | Database: PDB / ID: 1gmx | ||||||
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Title | Escherichia coli GlpE sulfurtransferase | ||||||
![]() | THIOSULFATE SULFURTRANSFERASE GLPE | ||||||
![]() | TRANSFERASE / RHODANESE / SULFURTRANSFERASE / GLYCEROL METABOLISM | ||||||
Function / homology | ![]() sulfur utilization / thiosulfate sulfurtransferase / glycerol metabolic process / thiosulfate sulfurtransferase activity / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Spallarossa, A. / Donahue, J.T. / Larson, T.J. / Bolognesi, M. / Bordo, D. | ||||||
![]() | ![]() Title: Escherichia Coli Glpe is a Prototype Sulfurtransferase for the Single-Domain Rhodanese Homology Superfamily Authors: Spallarossa, A. / Donahue, J.T. / Larson, T.J. / Bolognesi, M. / Bordo, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 57.1 KB | Display | ![]() |
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PDB format | ![]() | 45.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 446.8 KB | Display | ![]() |
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Full document | ![]() | 450.7 KB | Display | |
Data in XML | ![]() | 9.2 KB | Display | |
Data in CIF | ![]() | 11.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 12124.485 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||
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#2: Chemical | #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 42 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.60 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Date: Oct 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 1.06→20 Å / Num. obs: 45040 / % possible obs: 99.6 % / Observed criterion σ(I): 3 / Redundancy: 1.2 % / Rmerge(I) obs: 0.023 / Net I/σ(I): 43 |
Reflection shell | Resolution: 1.06→1.08 Å / Rmerge(I) obs: 0.281 / Mean I/σ(I) obs: 3 / % possible all: 93.6 |
Reflection | *PLUS Lowest resolution: 20 Å / Num. measured all: 555366 |
Reflection shell | *PLUS % possible obs: 93.6 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.1→47 Å
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Refinement | *PLUS Highest resolution: 1.06 Å / Lowest resolution: 47 Å / % reflection Rfree: 5 % / Rfactor obs: 0.128 / Rfactor Rfree: 0.151 / Rfactor Rwork: 0.128 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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