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- PDB-2o1g: Natural occurring mutant of Human ABO(H) Galactosyltransferase: G... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2o1g | ||||||
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Title | Natural occurring mutant of Human ABO(H) Galactosyltransferase: GTB/M214T | ||||||
![]() | ABO glycosyltransferase | ||||||
![]() | TRANSFERASE / Glycosyltransferase / GTB / blood type subgroups / naturally occuring mutant / DXD | ||||||
Function / homology | ![]() fucosylgalactoside 3-alpha-galactosyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity / fucosylgalactoside 3-alpha-galactosyltransferase activity / ABO blood group biosynthesis / lipid glycosylation / Golgi cisterna membrane / protein glycosylation / antigen binding / manganese ion binding ...fucosylgalactoside 3-alpha-galactosyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase / glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase activity / fucosylgalactoside 3-alpha-galactosyltransferase activity / ABO blood group biosynthesis / lipid glycosylation / Golgi cisterna membrane / protein glycosylation / antigen binding / manganese ion binding / vesicle / carbohydrate metabolic process / Golgi membrane / nucleotide binding / Golgi apparatus / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Letts, J.A. / Borisova, S.N. / Evans, S.V. | ||||||
![]() | ![]() Title: Structural effects of naturally occurring human blood group B galactosyltransferase mutations adjacent to the DXD motif. Authors: Persson, M. / Letts, J.A. / Hosseini-Maaf, B. / Borisova, S.N. / Palcic, M.M. / Evans, S.V. / Olsson, M.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.4 KB | Display | ![]() |
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PDB format | ![]() | 54.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 436.5 KB | Display | ![]() |
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Full document | ![]() | 440.2 KB | Display | |
Data in XML | ![]() | 14.3 KB | Display | |
Data in CIF | ![]() | 20.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2o1fC ![]() 2o1hC ![]() 1lz7S 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: 34496.754 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||
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#2: Chemical | ChemComp-HG / #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.65 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: ADA, manganese chloride, ammonium sulfate, MPD, glycerol, PEG 4000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Apr 21, 2006 |
Radiation | Monochromator: Osmic "Blue" confocal x-ray mirrors wit hpower levels of 30 watts Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.71→20 Å / Num. obs: 33405 / % possible obs: 96.7 % / Redundancy: 4.42 % / Rmerge(I) obs: 0.053 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 1.71→1.77 Å / Redundancy: 4.08 % / Rmerge(I) obs: 0.302 / Mean I/σ(I) obs: 3.8 / % possible all: 99.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1lz7 Resolution: 1.71→20 Å / Cor.coef. Fo:Fc: 0.965 / Cor.coef. Fo:Fc free: 0.949 / SU B: 2.006 / SU ML: 0.067 / Cross valid method: THROUGHOUT / ESU R: 0.106 / ESU R Free: 0.105 / 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: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 25.932 Å2
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Refinement step | Cycle: LAST / Resolution: 1.71→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.71→1.754 Å / Total num. of bins used: 20
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