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Open data
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Basic information
Entry | Database: PDB / ID: 2eib | ||||||
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Title | Crystal Structure of Galactose Oxidase, W290H mutant | ||||||
![]() | Galactose oxidase | ||||||
![]() | OXIDOREDUCTASE / Galactose Oxidase mutant | ||||||
Function / homology | ![]() galactose oxidase / galactose oxidase activity / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Phillips, S.E. / McPherson, M.J. / Knowles, P.F. / Wilmot, C. | ||||||
![]() | ![]() Title: The Stacking Tryptophan of Galactose Oxidase: A Second-Coordination Sphere Residue that Has Profound Effects on Tyrosyl Radical Behavior and Enzyme Catalysis Authors: Rogers, M.S. / Tyler, E.M. / Akyumani, N. / Kurtis, C.R. / Spooner, R.K. / Deacon, S.E. / Tamber, S. / Firbank, S.J. / Mahmoud, K. / Knowles, P.F. / Phillips, S.E. / McPherson, M.J. / Dooley, D.M. #1: Journal: J.Biol.Chem. / Year: 1994 Title: Structure and mechanism of galactose oxidase. The free radical site Authors: Baron, A.J. / Stevens, C. / Wilmot, C. / Seneviratne, K.D. / Blakeley, V. / Dooley, D.M. / Phillips, S.E. / Knowles, P.F. / McPherson, M.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 143.6 KB | Display | ![]() |
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PDB format | ![]() | 108 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 392.4 KB | Display | ![]() |
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Full document | ![]() | 423.9 KB | Display | |
Data in XML | ![]() | 17.8 KB | Display | |
Data in CIF | ![]() | 27.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2eicC ![]() 2eidC ![]() 2eieC ![]() 1gogS 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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1 |
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Unit cell |
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Details | Protein is a monomer in the asymmetric unit |
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Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 68530.531 Da / Num. of mol.: 1 / Fragment: residues 1-639 / Mutation: W290H Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q01745, UniProt: P0CS93*PLUS, galactose oxidase |
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-Non-polymers , 5 types, 332 molecules ![](data/chem/img/CU.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ACT.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-CU / | ||
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#3: Chemical | ChemComp-NA / | ||
#4: Chemical | ChemComp-SO4 / | ||
#5: Chemical | #6: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.9 Å3/Da / Density % sol: 74.9 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: 1-2M Amonium Sulphate, 0.1M sodium acetate pH 4-5, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: SIEMENS-NICOLET X100 / Detector: AREA DETECTOR |
Radiation | Monochromator: Graphite / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Rsym value: 0.046 |
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Processing
Software | Name: PROLSQ / Classification: refinement | ||||||||||||
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Refinement | Method to determine structure: ![]() Starting model: 1GOG Resolution: 2.1→10 Å / Rfactor Rwork: 0.157 / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber | ||||||||||||
Displacement parameters | Biso mean: 24.376 Å2 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→10 Å
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Refine LS restraints | Type: p_bond_d / Dev ideal: 0.017 |