1wgt: Difference between revisions
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[[Image:1wgt.gif|left|200px]] | [[Image:1wgt.gif|left|200px]] | ||
'''X-RAY STRUCTURE OF WHEAT GERM AGGLUTININ ISOLECTIN 3''' | {{Structure | ||
|PDB= 1wgt |SIZE=350|CAPTION= <scene name='initialview01'>1wgt</scene>, resolution 1.90Å | |||
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'''X-RAY STRUCTURE OF WHEAT GERM AGGLUTININ ISOLECTIN 3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1WGT is a [ | 1WGT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WGT OCA]. | ||
==Reference== | ==Reference== | ||
X-ray structure of wheat germ agglutinin isolectin 3., Harata K, Nagahora H, Jigami Y, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1013-9. PMID:[http:// | X-ray structure of wheat germ agglutinin isolectin 3., Harata K, Nagahora H, Jigami Y, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1013-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299769 15299769] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Triticum aestivum]] | [[Category: Triticum aestivum]] | ||
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[[Category: lectin (agglutinin)]] | [[Category: lectin (agglutinin)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:56:50 2008'' | ||
Revision as of 12:56, 20 March 2008
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| 1wgt, resolution 1.90Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
X-RAY STRUCTURE OF WHEAT GERM AGGLUTININ ISOLECTIN 3
Overview
Wheat germ agglutinin isolectin 3 (WGA3) was crystallized from 10 mM acetate buffer at pH 4.9 containing 6 mM CaCl(2) and 4%(v/v) ethanol. The crystal belongs to monoclinic space group P2(1) with unit-cell dimensions a = 44.86, b = 91.02, c = 44.86 A, and beta = 110.22 degrees. The asymmetric unit contains two molecules (V(m) = 2.51 A(3) Da(-1)). The crystal structure was solved by the molecular-replacement method and was refined by the simulated-annealing method. The conventional R value was 0.191 for 19713 reflections [|F(o)| > 3sigma(F)] in the resolution range 8-1.9 A. The r.m.s. deviations from the ideal bond distances and angles were 0.014 A, and 3.0 degrees, respectively, and the estimated coordinate error was 0.2-0.25 A. The two molecules in the asymmetric unit are related by the pseudo twofold symmetry and form a dimer structure. The backbone structures of the two subunits are nearly identical with the r.m.s. difference of 0.36 A for the superposition of equivalent C(alpha) atoms. The dimer structure is very similar to those of isolectins 1 and 2 with the r.m.s. difference of 0.35-0.39 A for the C(alpha) superposition. Since amino-acid residues which differ from those of isolectin 1 or 2 are not involved in the contact between the two subunits, the subunit-subunit interaction is not significantly affected by the replacement of these residues. As a result, the geometry of the sugar-binding sites which are located at the interface between the two subunit molecules is basically conserved among three isolectins.
About this Structure
1WGT is a Single protein structure of sequence from Triticum aestivum. Full crystallographic information is available from OCA.
Reference
X-ray structure of wheat germ agglutinin isolectin 3., Harata K, Nagahora H, Jigami Y, Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):1013-9. PMID:15299769
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