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- PDB-2xh7: Engineering the enolase active site pocket: Crystal structure of ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2xh7 | ||||||
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Title | Engineering the enolase active site pocket: Crystal structure of the D321A mutant of yeast enolase 1 | ||||||
![]() | ENOLASE 1 | ||||||
![]() | LYASE / TIM-BARREL / ENOLASE SUPERFAMILY / GLYCOLYSIS / GLUCONEOGENESIS / METAL BINDING | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Schreier, B. / Hocker, B. | ||||||
![]() | ![]() Title: Engineering the Enolase Magnesium II Binding Site -Implications for its Evolution. Authors: Schreier, B. / Hoecker, B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 191.7 KB | Display | ![]() |
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PDB format | ![]() | 150 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2xgzC ![]() 2xh0C ![]() 2xh2C ![]() 2xh4SC C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47644.844 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-437 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: PET-21 / Production host: ![]() ![]() #2: Chemical | ChemComp-MG / #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.85 % / Description: NONE |
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Crystal grow | pH: 8 Details: 18% PEG 6000, 0.2M MAGNESIUM CHLORIDE, 0.1M TRIS PH 8.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 27, 2009 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. obs: 73622 / % possible obs: 91.3 % / Observed criterion σ(I): 2 / Redundancy: 1.81 % / Biso Wilson estimate: 26.5 Å2 / Rmerge(I) obs: 0.15 / Net I/σ(I): 11.43 |
Reflection shell | Resolution: 1.8→1.91 Å / Redundancy: 1.75 % / Rmerge(I) obs: 0.68 / Mean I/σ(I) obs: 3.12 / % possible all: 89.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2XH4 Resolution: 1.8→43.69 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.94 / SU B: 2.585 / SU ML: 0.082 / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.13 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.06 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→43.69 Å
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Refine LS restraints |
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