[English] 日本語
Yorodumi- PDB-1zi3: Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1zi3 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Crystal Structure of Human N-acetylgalactosaminyltransferase (GTA) Complexed with N-acetyllactosamine | |||||||||
Components | Histo-blood group ABO system transferase (NAGAT) Includes: Glycoprotein-fucosylgalactoside alpha-N- acetylgalactosaminyltransferase | |||||||||
Keywords | TRANSFERASE / GTA / ABO(H) / H-antigen / blood groups / glycosyltransferase | |||||||||
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: 1.69 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1zi3.cif.gz | 74.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1zi3.ent.gz | 53.1 KB | Display | PDB format |
PDBx/mmJSON format | 1zi3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/zi/1zi3 ftp://data.pdbj.org/pub/pdb/validation_reports/zi/1zi3 | HTTPS FTP |
---|
-Related structure data
Related structure data | 1zhjC 1zi1C 1zi4C 1zi5C 1zizC 1zj0C 1zj1C 1zj2C 1zj3C 1zjoC 1zjpC 2a8uC 2a8wC 1lz0S C: citing same article (ref.) S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-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 | ||||
---|---|---|---|---|---|
#2: Polysaccharide | beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose / N-acetyl-alpha-lactosamine | ||||
#3: Chemical | ChemComp-HG / #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.84 % |
---|
-Data collection
Diffraction | Mean temperature: 113 K |
---|---|
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Feb 18, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
-Processing
Software |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1LZ0 Resolution: 1.69→20 Å /
| ||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.69→20 Å
|