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Open data
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Basic information
Entry | Database: PDB / ID: 1l8p | ||||||
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Title | Mg-phosphonoacetohydroxamate complex of S39A yeast enolase 1 | ||||||
![]() | enolase 1 | ||||||
![]() | LYASE / Beta Barrel | ||||||
Function / homology | ![]() Gluconeogenesis / regulation of vacuole fusion, non-autophagic / Glycolysis / melatonin binding / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / fungal-type vacuole / glycolytic process / magnesium ion binding ...Gluconeogenesis / regulation of vacuole fusion, non-autophagic / Glycolysis / melatonin binding / phosphopyruvate hydratase / phosphopyruvate hydratase complex / phosphopyruvate hydratase activity / fungal-type vacuole / glycolytic process / magnesium ion binding / mitochondrion / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Poyner, R.R. / Larsen, T.M. / Wong, S.W. / Reed, G.H. | ||||||
![]() | ![]() Title: Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase. Authors: Poyner, R.R. / Larsen, T.M. / Wong, S.W. / Reed, G.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 365.1 KB | Display | ![]() |
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PDB format | ![]() | 290.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 402.8 KB | Display | ![]() |
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Full document | ![]() | 419.7 KB | Display | |
Data in XML | ![]() | 34.6 KB | Display | |
Data in CIF | ![]() | 59.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 46716.797 Da / Num. of mol.: 4 / Mutation: S39A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: eno1 / Plasmid: pET22B / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Chemical | ChemComp-MG / #3: Chemical | ChemComp-PAH / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.59 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 8 Details: PEG 8000, Potassium Chloride, HEPPs, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 292K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: batch method / Details: used microseeding | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: CUSTOM-MADE / Detector: CCD / Date: Sep 13, 2000 |
Radiation | Monochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.0332 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→20 Å / Num. all: 97095 / Num. obs: 97095 / % possible obs: 96.8 % / Observed criterion σ(I): -3 / Rmerge(I) obs: 0.031 |
Reflection shell | Resolution: 2.1→2.17 Å / % possible all: 96.8 |
Reflection | *PLUS Highest resolution: 2.1 Å / Lowest resolution: 20 Å / Num. measured all: 266980 / Rmerge(I) obs: 0.031 |
Reflection shell | *PLUS Highest resolution: 2.1 Å / % possible obs: 96.2 % / Rmerge(I) obs: 0.049 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.1→20 Å
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Refine LS restraints |
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Refinement | *PLUS Lowest resolution: 20 Å / Rfactor obs: 0.181 / Rfactor Rfree: 0.223 / Rfactor Rwork: 0.181 | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS |