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- PDB-1wt1: Mutant ABO(H) blood group glycosyltransferase with bound UDP and ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1wt1 | |||||||||
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Title | Mutant ABO(H) blood group glycosyltransferase with bound UDP and acceptor | |||||||||
![]() | Histo-blood group ABO system transferase | |||||||||
![]() | TRANSFERASE | |||||||||
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 | ![]() ![]() | |||||||||
![]() | Lee, H.J. / Barry, C.H. / Borisova, S.N. / Seto, N.O.L. / Zheng, R.B. / Blancher, A. / Evans, S.V. / Palcic, M.M. | |||||||||
![]() | ![]() Title: Structural basis for the inactivity of human blood group o2 glycosyltransferase Authors: Lee, H.J. / Barry, C.H. / Borisova, S.N. / Seto, N.O.L. / Zheng, R.B. / Blancher, A. / Evans, S.V. / Palcic, M.M. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 75.6 KB | Display | ![]() |
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PDB format | ![]() | 53.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1011.4 KB | Display | ![]() |
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Full document | ![]() | 1018.5 KB | Display | |
Data in XML | ![]() | 15.2 KB | Display | |
Data in CIF | ![]() | 21.8 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34147.465 Da / Num. of mol.: 1 / Fragment: residues 63-354 / Mutation: G268R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P16442, glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase | ||||
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#2: Polysaccharide | alpha-L-fucopyranose-(1-2)-hexyl beta-D-galactopyranoside Type: oligosaccharide / Mass: 410.456 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source | ||||
#3: Chemical | ChemComp-HG / #4: Chemical | ChemComp-UDP / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.64 % |
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: SEALED TUBE / Type: RIGAKU / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
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Processing
Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 1.55→20 Å
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