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Yorodumi- PDB-1zi1: Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zi1 | ||||||
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Title | Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with Lactose | ||||||
Components | Histo-blood group ABO system transferase (NAGAT) Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase | ||||||
Keywords | TRANSFERASE / GTA / ABO(H) / H-antigen / Blood groups | ||||||
Function / homology | Function and homology information 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 | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.57 Å | ||||||
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. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2006 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1zi1.cif.gz | 73.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1zi1.ent.gz | 53.2 KB | Display | PDB format |
PDBx/mmJSON format | 1zi1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zi/1zi1 ftp://data.pdbj.org/pub/pdb/validation_reports/zi/1zi1 | HTTPS FTP |
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-Related structure data
Related structure data | 1zhjC 1zi3C 1zi4C 1zi5C 1zizC 1zj0C 1zj1C 1zj2C 1zj3C 1zjoC 1zjpC 2a8uC 2a8wC 1lz0S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-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: 34194.496 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ABO / Plasmid: pcw delta 1ac (E/H) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21Gold 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: X-RAY DIFFRACTION / Number of used crystals: 1 |
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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 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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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