4c7d - Revision history

OCA at 12:05, 20 December 2023

OCA — Wed, 20 Dec 2023 12:05:25 GMT

←Older revision		Revision as of 12:05, 20 December 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.85Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [https://pdbe.org/4c7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [https://www.ebi.ac.uk/pdbsum/4c7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7d ProSAT]</span></td></tr>		<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [https://pdbe.org/4c7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [https://www.ebi.ac.uk/pdbsum/4c7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7d ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/Q9L068_STRCO Q9L068_STRCO]]	+	[https://www.uniprot.org/uniprot/Q9L068_STRCO Q9L068_STRCO]
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-N-acetylhexosaminidases (HEX) are glycosidases that catalyze the glycosidic linkage hydrolysis of gluco- and galacto-configured N-acetyl-beta-D-hexosaminides. These enzymes are important in human physiology and are candidates for the biocatalytic production of carbohydrates and glycomimetics. In this study, the three-dimensional structure of the wild-type and catalytically impaired E302Q HEX variant from the soil bacterium Streptomyces coelicolor A3(2) (ScHEX) were solved in ligand-free forms and in the presence of 6-acetamido-6-deoxy-castanospermine (6-Ac-Cas). The E302Q variant was also trapped as an intermediate with oxazoline bound to the active center. Crystallographic evidence highlights structural variations in the loop 3 environment, suggesting conformational heterogeneity for important active-site residues of this GH20 family member. The enzyme was investigated for its beta-N-acetylhexosaminidase activity toward chitooligomers and pNP-acetyl gluco- and galacto-configured N-acetyl hexosaminides. Kinetic analyses confirm the beta(1-4) glycosidic linkage substrate preference and HPLC profiles support an exoglycosidase mechanism, where the enzyme cleaves sugars from the non-reducing end of substrates. ScHEX possesses significant activity toward chitooligosaccharides of varying degrees of polymerization and the final hydrolytic reaction yielded pure GlcNAc without any byproduct, promising high applicability for the enzymatic production of this highly valued chemical. Thermostability and activation assays further suggest efficient conditions applicable to the enzymatic production of GlcNAc from chitooligomers.
		+
		+	Structure and activity of the Streptomyces coelicolor A3(2) beta-N-acetylhexosaminidase provides further insight into GH20 family catalysis and inhibition.,Nguyen Thi N, Offen WA, Shareck F, Davies GJ, Doucet N Biochemistry. 2014 Feb 21. PMID:24559145<ref>PMID:24559145</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4c7d" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Beta-N-acetylhexosaminidase 3D structures\|Beta-N-acetylhexosaminidase 3D structures]]		*[[Beta-N-acetylhexosaminidase 3D structures\|Beta-N-acetylhexosaminidase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 17:30, 7 September 2022

OCA — Wed, 07 Sep 2022 17:30:26 GMT

←Older revision		Revision as of 17:30, 7 September 2022
Line 3:		Line 3:
	<StructureSection load='4c7d' size='340' side='right'caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='4c7d' size='340' side='right'caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces~~ coelicolor~~" (muller 1908) lieske 1921~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4C7D FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor Streptomyces coelicolor]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C7D FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c7f\|4c7f]], [[4c7g\|4c7g]]</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [https://pdbe.org/4c7d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [https://www.ebi.ac.uk/pdbsum/4c7d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7d ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [~~http~~://pdbe.org/4c7d PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4c7d PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7d ProSAT]</span></td></tr>	+
	</table>		</table>
-	~~<div style~~=~~"background-color:#fffaf0;">~~	+	== Function ==
-	=~~= Publication Abstract from PubMed~~ ==	+	[[https://www.uniprot.org/uniprot/Q9L068_STRCO Q9L068_STRCO]]
-	beta-N-acetylhexosaminidases (HEX) are glycosidases that catalyze the glycosidic linkage hydrolysis of gluco- and galacto-configured N-acetyl-beta-D-hexosaminides. These enzymes are important in human physiology and are candidates for the biocatalytic production of carbohydrates and glycomimetics. In this study, the three-dimensional structure of the wild-type and catalytically impaired E302Q HEX variant from the soil bacterium Streptomyces coelicolor A3(2) (ScHEX) were solved in ligand-free forms and in the presence of 6-acetamido-6-deoxy-castanospermine (6-Ac-Cas). The E302Q variant was also trapped as an intermediate with oxazoline bound to the active center. Crystallographic evidence highlights structural variations in the loop 3 environment, suggesting conformational heterogeneity for important active-site residues of this GH20 family member. The enzyme was investigated for its beta-N-acetylhexosaminidase activity toward chitooligomers and pNP-acetyl gluco- and galacto-configured N-acetyl hexosaminides. Kinetic analyses confirm the beta(1-4) glycosidic linkage substrate preference and HPLC profiles support an exoglycosidase mechanism, where the enzyme cleaves sugars from the non-reducing end of substrates. ScHEX possesses significant activity toward chitooligosaccharides of varying degrees of polymerization and the final hydrolytic reaction yielded pure GlcNAc without any byproduct, promising high applicability for the enzymatic production of this highly valued chemical. ~~Thermostability and activation assays further suggest efficient conditions applicable to the enzymatic production of GlcNAc from chitooligomers~~.	+

-	~~Structure and activity of the Streptomyces coelicolor A3(2) beta~~-N-acetylhexosaminidase ~~provides further insight into GH20 family catalysis and inhibition.,Nguyen Thi~~ N~~, Offen WA, Shareck F, Davies GJ, Doucet N Biochemistry. 2014 Feb 21. PMID:24559145<ref>PMID:24559145</ref>~~	+	==See Also==
-		+	*[[Beta-N-acetylhexosaminidase 3D structures\|Beta-N-acetylhexosaminidase 3D structures]]
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe~~-~~citations 4c7d" style="background-color:#fffaf0;"></div>~~	+
-	~~== References ==~~	+
-	~~<references/>~~	+
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Beta-N-acetylhexosaminidase]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Davies, G J~~]]	+	[[Category: Streptomyces coelicolor]]
-	[[Category: ~~Doucet, N~~]]	+	[[Category: Davies GJ]]
-	[[Category: ~~Nguyenthi,~~ N]]	+	[[Category: Doucet N]]
-	[[Category: ~~Offen, W A~~]]	+	[[Category: Nguyenthi N]]
-	[[Category: ~~Hydrolase~~]]	+	[[Category: Offen WA]]

OCA at 16:25, 28 August 2019

OCA — Wed, 28 Aug 2019 16:25:10 GMT

←Older revision		Revision as of 16:25, 28 August 2019
Line 1:		Line 1:

	==Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)==		==Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)==
-	<StructureSection load='4c7d' size='340' side='right' caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>	+	<StructureSection load='4c7d' size='340' side='right'caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7D FirstGlance]. <br>		<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7D FirstGlance]. <br>
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
		+	[[Category: Large Structures]]
	[[Category: Davies, G J]]		[[Category: Davies, G J]]
	[[Category: Doucet, N]]		[[Category: Doucet, N]]

OCA at 19:44, 11 August 2016

OCA — Thu, 11 Aug 2016 19:44:33 GMT

←Older revision		Revision as of 19:44, 11 August 2016
Line 1:		Line 1:
		+
	==Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)==		==Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)==
	<StructureSection load='4c7d' size='340' side='right' caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>		<StructureSection load='4c7d' size='340' side='right' caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c7f\|4c7f]], [[4c7g\|4c7g]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c7f\|4c7f]], [[4c7g\|4c7g]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [http://www.ebi.ac.uk/pdbsum/4c7d PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [http://pdbe.org/4c7d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [http://www.ebi.ac.uk/pdbsum/4c7d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c7d ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 16:		Line 17:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4c7d" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:33, 4 January 2015

OCA — Sun, 04 Jan 2015 12:33:33 GMT

←Older revision		Revision as of 12:33, 4 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4c7d\| PDB=4c7d \| SCENE= }}~~	+	==Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)==
-	===Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)===	+	<StructureSection load='4c7d' size='340' side='right' caption='[[4c7d]], [[Resolution\|resolution]] 1.85Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24559145}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4c7d]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_coelicolor"_(muller_1908)_lieske_1921 "actinomyces coelicolor" (muller 1908) lieske 1921]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C7D FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4c7f\|4c7f]], [[4c7g\|4c7g]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-N-acetylhexosaminidase Beta-N-acetylhexosaminidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.52 3.2.1.52] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4c7d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c7d OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4c7d RCSB], [http://www.ebi.ac.uk/pdbsum/4c7d PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	beta-N-acetylhexosaminidases (HEX) are glycosidases that catalyze the glycosidic linkage hydrolysis of gluco- and galacto-configured N-acetyl-beta-D-hexosaminides. These enzymes are important in human physiology and are candidates for the biocatalytic production of carbohydrates and glycomimetics. In this study, the three-dimensional structure of the wild-type and catalytically impaired E302Q HEX variant from the soil bacterium Streptomyces coelicolor A3(2) (ScHEX) were solved in ligand-free forms and in the presence of 6-acetamido-6-deoxy-castanospermine (6-Ac-Cas). The E302Q variant was also trapped as an intermediate with oxazoline bound to the active center. Crystallographic evidence highlights structural variations in the loop 3 environment, suggesting conformational heterogeneity for important active-site residues of this GH20 family member. The enzyme was investigated for its beta-N-acetylhexosaminidase activity toward chitooligomers and pNP-acetyl gluco- and galacto-configured N-acetyl hexosaminides. Kinetic analyses confirm the beta(1-4) glycosidic linkage substrate preference and HPLC profiles support an exoglycosidase mechanism, where the enzyme cleaves sugars from the non-reducing end of substrates. ScHEX possesses significant activity toward chitooligosaccharides of varying degrees of polymerization and the final hydrolytic reaction yielded pure GlcNAc without any byproduct, promising high applicability for the enzymatic production of this highly valued chemical. Thermostability and activation assays further suggest efficient conditions applicable to the enzymatic production of GlcNAc from chitooligomers.

-	~~==About this~~ Structure==	+	Structure and activity of the Streptomyces coelicolor A3(2) beta-N-acetylhexosaminidase provides further insight into GH20 family catalysis and inhibition.,Nguyen Thi N, Offen WA, Shareck F, Davies GJ, Doucet N Biochemistry. 2014 Feb 21. PMID:24559145<ref>PMID:24559145</ref>
-	~~[[4c7d]] is a~~ 2 ~~chain structure~~. ~~Full crystallographic information is available from [http://oca~~.~~weizmann~~.~~ac.il~~/~~oca-bin/ocashort?id=4C7D OCA].~~	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024559145</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Beta-N-acetylhexosaminidase]]		[[Category: Beta-N-acetylhexosaminidase]]
-	[[Category: Davies, G J.]]	+	[[Category: Davies, G J]]
-	[[Category: Doucet, N.]]	+	[[Category: Doucet, N]]
-	[[Category: Nguyenthi, N.]]	+	[[Category: Nguyenthi, N]]
-	[[Category: Offen, W A.]]	+	[[Category: Offen, W A]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 13:51, 12 March 2014

OCA — Wed, 12 Mar 2014 13:51:36 GMT

←Older revision		Revision as of 13:51, 12 March 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4c7d\| PDB=4c7d \| SCENE= }}
		+	===Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)===
		+	{{ABSTRACT_PUBMED_24559145}}

-	~~The entry~~ 4c7d is ~~ON HOLD until Paper Publication~~	+	==About this Structure==
		+	[[4c7d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C7D OCA].

-	~~Authors~~: ~~Nguyenthi,~~ N~~., Offen, W.A.,~~ Davies, G.J., Doucet, N.	+	==Reference==
-		+	<ref group="xtra">PMID:024559145</ref><references group="xtra"/><references/>
-	~~Description~~: ~~Structure and activity of the GH20 beta-~~N~~-acetylhexosaminidase from Streptomyces coelicolor A3(2)~~	+	[[Category: Beta-N-acetylhexosaminidase]]
		+	[[Category: Davies, G J.]]
		+	[[Category: Doucet, N.]]
		+	[[Category: Nguyenthi, N.]]
		+	[[Category: Offen, W A.]]
		+	[[Category: Hydrolase]]

OCA at 04:44, 13 February 2014

OCA — Thu, 13 Feb 2014 04:44:01 GMT

←Older revision		Revision as of 04:44, 13 February 2014
Line 3:		Line 3:
	The entry 4c7d is ON HOLD until Paper Publication		The entry 4c7d is ON HOLD until Paper Publication

-	Authors: ~~Nguyen Thi~~, N., Offen, W.A., Davies, G.J., Doucet, N.	+	Authors: Nguyenthi, N., Offen, W.A., Davies, G.J., Doucet, N.

	Description: Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)		Description: Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)

OCA at 06:33, 2 October 2013

OCA — Wed, 02 Oct 2013 06:33:25 GMT

←Older revision		Revision as of 06:33, 2 October 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4c7d is ON HOLD until ~~sometime in the future~~	+	The entry 4c7d is ON HOLD until Paper Publication

-	Authors: ~~Nguyenthi~~, N., Offen, W.A., Davies, G.J., Doucet, N.	+	Authors: Nguyen Thi, N., Offen, W.A., Davies, G.J., Doucet, N.

	Description: Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)		Description: Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)

OCA: Protected "4c7d" [edit=sysop:move=sysop]

OCA — Sun, 29 Sep 2013 07:17:14 GMT

Protected "4c7d" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:17, 29 September 2013

OCA: New page: '''Unreleased structure''' The entry 4c7d is ON HOLD until sometime in the future Authors: Nguyenthi, N., Offen, W.A., Davies, G.J., Doucet, N. Description: Structure and activity of t...

OCA — Sun, 29 Sep 2013 07:17:13 GMT

New page: '''Unreleased structure''' The entry 4c7d is ON HOLD until sometime in the future Authors: Nguyenthi, N., Offen, W.A., Davies, G.J., Doucet, N. Description: Structure and activity of t...

New page

'''Unreleased structure'''

The entry 4c7d is ON HOLD until sometime in the future

Authors: Nguyenthi, N., Offen, W.A., Davies, G.J., Doucet, N.

Description: Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces coelicolor A3(2)