1k7c: Difference between revisions

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[[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1k7c, resolution 1.12Å" />

'''Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution'''<br />

==Overview==

The crystal structure of the glycoprotein rhamnogalacturonan, acetylesterase from Aspergillus aculeatus has been refined to a resolution, of 1.12 A using synchrotron data collected at 263 K. Both of the two, putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally, well defined in the electron-density maps, showing the six-carbohydrate, structure, Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn18, 2. Equivalent carbohydrate residues were restrained to have similar, geometries, but were refined without target values. The refined bond, lengths and angles were compared with the values obtained from, small-molecule studies that form the basis for the dictionaries used for, glycoprotein refinement.

The crystal structure of the glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been refined to a resolution of 1.12 A using synchrotron data collected at 263 K. Both of the two putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally well defined in the electron-density maps, showing the six-carbohydrate structure Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn18 2. Equivalent carbohydrate residues were restrained to have similar geometries, but were refined without target values. The refined bond lengths and angles were compared with the values obtained from small-molecule studies that form the basis for the dictionaries used for glycoprotein refinement.

==About this Structure==

1K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1K7C OCA].

1K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K7C OCA].

==Reference==

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[[Category: sgnh-hydrolase]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 18~~:54:~~57 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:55 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1k7c.jpg|left|200px]]<br /><applet load="1k7c" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1k7c, resolution 1.12&Aring;" />
 '''Rhamnogalacturonan acetylesterase with seven N-linked carbohydrate residues distributed at two N-glycosylation sites refined at 1.12 A resolution'''<br />
 ==Overview==
-The crystal structure of the glycoprotein rhamnogalacturonan, acetylesterase from Aspergillus aculeatus has been refined to a resolution, of 1.12 A using synchrotron data collected at 263 K. Both of the two, putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally, well defined in the electron-density maps, showing the six-carbohydrate, structure, Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn18, 2. Equivalent carbohydrate residues were restrained to have similar, geometries, but were refined without target values. The refined bond, lengths and angles were compared with the values obtained from, small-molecule studies that form the basis for the dictionaries used for, glycoprotein refinement.
+The crystal structure of the glycoprotein rhamnogalacturonan acetylesterase from Aspergillus aculeatus has been refined to a resolution of 1.12 A using synchrotron data collected at 263 K. Both of the two putative N-glycosylation sites at Asn104 and Asn182 are glycosylated and, owing to crystal contacts, the glycan structure at Asn182 is exceptionally well defined in the electron-density maps, showing the six-carbohydrate structure Manalpha1-6(Manalpha1-3)Manalpha1-6Manbeta1-4GlcNAcbeta1-4GlcNAcbeta-Asn18 2. Equivalent carbohydrate residues were restrained to have similar geometries, but were refined without target values. The refined bond lengths and angles were compared with the values obtained from small-molecule studies that form the basis for the dictionaries used for glycoprotein refinement.
 ==About this Structure==
-K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K7C OCA].
+K7C is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aspergillus_aculeatus Aspergillus aculeatus] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K7C OCA].
 ==Reference==
@@ Line 20: / Line 20: @@
 [[Category: sgnh-hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:54:57 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:55 2008''