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- PDB-1zi1: Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1zi1 | ||||||
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Title | Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Lactose | ||||||
![]() | Histo-blood group ABO system transferase (NAGAT) Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase | ||||||
![]() | TRANSFERASE / GTA / ABO(H) / H-antigen / Blood groups | ||||||
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. / Rose, N.L. / Fang, Y.R. / Barry, C.H. / Borisova, S.N. / Seto, N.O. / Palcic, M.M. / Evans, S.V. | ||||||
![]() | ![]() Title: Differential Recognition of the Type I and II H Antigen Acceptors by the Human ABO(H) Blood Group A and B Glycosyltransferases. Authors: Letts, J.A. / Rose, N.L. / Fang, Y.R. / Barry, C.H. / Borisova, S.N. / Seto, N.O. / Palcic, M.M. / Evans, S.V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 73.6 KB | Display | ![]() |
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PDB format | ![]() | 53.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438 KB | Display | ![]() |
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Full document | ![]() | 444.3 KB | Display | |
Data in XML | ![]() | 14.8 KB | Display | |
Data in CIF | ![]() | 21.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zhjC ![]() 1zi3C ![]() 1zi4C ![]() 1zi5C ![]() 1zizC ![]() 1zj0C ![]() 1zj1C ![]() 1zj2C ![]() 1zj3C ![]() 1zjoC ![]() 1zjpC ![]() 2a8uC ![]() 2a8wC ![]() 1lz0S 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34194.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P16442, glycoprotein-fucosylgalactoside alpha-N-acetylgalactosaminyltransferase | ||||||
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#2: Chemical | ChemComp-HG / #3: Chemical | ChemComp-CL / | #4: Chemical | ChemComp-MN / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.29 Å3/Da / Density % sol: 46.18 % |
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-Data collection
Diffraction | Mean temperature: 113 K |
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Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 10, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1LZ0 Resolution: 1.57→20 Å Details: Long C-N bond length between Glu 197 and Arg 198 is the result of disorder in this region
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Refinement step | Cycle: LAST / Resolution: 1.57→20 Å
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