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Open data
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Basic information
Entry | Database: PDB / ID: 1zag | |||||||||
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Title | HUMAN ZINC-ALPHA-2-GLYCOPROTEIN | |||||||||
![]() | PROTEIN (ZINC-ALPHA-2-GLYCOPROTEIN) | |||||||||
![]() | LIPID MOBILIZATION FACTOR / SECRETED MHC CLASS I HOMOLOG | |||||||||
Function / homology | ![]() Miscellaneous transport and binding events / detection of chemical stimulus involved in sensory perception of bitter taste / protein transmembrane transporter activity / RNA nuclease activity / collagen-containing extracellular matrix / cell adhesion / immune response / negative regulation of cell population proliferation / external side of plasma membrane / extracellular space ...Miscellaneous transport and binding events / detection of chemical stimulus involved in sensory perception of bitter taste / protein transmembrane transporter activity / RNA nuclease activity / collagen-containing extracellular matrix / cell adhesion / immune response / negative regulation of cell population proliferation / external side of plasma membrane / extracellular space / extracellular exosome / extracellular region / nucleus Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Chirino, A.J. / Sanchez, L.M. / Bjorkman, P.J. | |||||||||
![]() | ![]() Title: Crystal structure of human ZAG, a fat-depleting factor related to MHC molecules. Authors: Sanchez, L.M. / Chirino, A.J. / Bjorkman, P. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 1997 Title: Biochemical characterization and crystalization of human Zn-alpha2-glycoprotein, a soluble class I major histocompatibility complex homolog. Authors: Sanchez, L.M. / Lopez-Otin, C. / Bjorkman, P.J. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1988 Title: Complete amino acid sequence of human plasma Zn-alpha 2-glycoprotein and its homology to histocompatibility antigens. Authors: Araki, T. / Gejyo, F. / Takagaki, K. / Haupt, H. / Schwick, H.G. / Burgi, W. / Marti, T. / Schaller, J. / Rickli, E. / Brossmer, R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 236.8 KB | Display | ![]() |
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PDB format | ![]() | 194.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 735.4 KB | Display | ![]() |
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Full document | ![]() | 771.6 KB | Display | |
Data in XML | ![]() | 28.5 KB | Display | |
Data in CIF | ![]() | 41.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS oper:
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Components
-Protein / Non-polymers , 2 types, 8 molecules ABCD![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#1: Protein | Mass: 31684.404 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Water | ChemComp-HOH / | |
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-Sugars , 5 types, 12 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / ZN-ALPHA-2-GLYCOPROTEIN / ZAG Source method: isolated from a genetically manipulated source |
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#3: Polysaccharide | N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D- ...N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / ZN-ALPHA-2-GLYCOPROTEIN / ZAG Source method: isolated from a genetically manipulated source |
#4: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / ZN-ALPHA-2-GLYCOPROTEIN / ZAG Source method: isolated from a genetically manipulated source |
#5: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / ZN-ALPHA-2-GLYCOPROTEIN / ZAG Source method: isolated from a genetically manipulated source |
#6: Sugar | ChemComp-NAG / |
-Details
Nonpolymer details | NO ATTEMPT HAS BEEN MADE TO MODEL OR OTHERWISE TAKE THE UNKNOWN LIGAND'S DENSITY INTO ACCOUNT ...NO ATTEMPT HAS BEEN MADE TO MODEL OR OTHERWISE TAKE THE UNKNOWN LIGAND'S DENSITY INTO ACCOUNT DURING REFINEMENT |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.2 Å3/Da / Density % sol: 63 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 5 Details: CRYSTALS WERE GROWN USING THE VAPOR DIFFUSION METHOD WITH 30% POLYETHYLENE GLYCOL 2000 MONOMETHYLETHER, 0.2M AMMONIUM ACETATE, AND 0.1M SODIUM ACETATE BUFFER (PH 5.0) | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7 / Method: vapor diffusionDetails: Sanchez, L.M., (1997) Proc.Nat.Acad.Sci.USA, 94, 4626. | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Mar 1, 1998 / Details: YALE MIRRORS |
Radiation | Monochromator: YALE MIRRORS / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→100 Å / Num. obs: 39365 / % possible obs: 95.6 % / Redundancy: 4.3 % / Biso Wilson estimate: 64.2 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 27 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.453 / Mean I/σ(I) obs: 2.5 / % possible all: 75.7 |
Reflection shell | *PLUS % possible obs: 75.7 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 15.15 Å2 / ksol: 0.26 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 54.3 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION / Weight Biso : 2 / Weight position: 300
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LS refinement shell | Resolution: 2.8→2.9 Å / Rfactor Rfree error: 0.034 / Total num. of bins used: 10
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Xplor file |
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Software | *PLUS Name: CNS / Version: 0.4 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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