4hk9 - Revision history

OCA at 11:42, 1 March 2024

OCA — Fri, 01 Mar 2024 11:42:01 GMT

←Older revision		Revision as of 11:42, 1 March 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4hk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HK9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4hk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HK9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900117:4beta-beta-xylotriose'>PRD_900117</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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]] 1.55Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900117:4beta-beta-xylotriose'>PRD_900117</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [https://pdbe.org/4hk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk9 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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [https://pdbe.org/4hk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/XYN2_HYPJR XYN2_HYPJR] Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).<ref>PMID:1369024</ref> <ref>PMID:19556747</ref> <ref>PMID:7988708</ref> <ref>PMID:1369024</ref>		[https://www.uniprot.org/uniprot/XYN2_HYPJR XYN2_HYPJR] Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).<ref>PMID:1369024</ref> <ref>PMID:19556747</ref> <ref>PMID:7988708</ref> <ref>PMID:1369024</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Xylanases catalyze the hydrolysis of plant hemicellulose xylan into oligosaccharides by cleaving the main-chain glycosidic linkages connecting xylose subunits. To study ligand binding and to understand how the pH constrains the activity of the enzyme, variants of the Trichoderma reesei xylanase were designed to either abolish its activity (E177Q) or to change its pH optimum (N44H). An E177Q-xylohexaose complex structure was obtained at 1.15 A resolution which represents a pseudo-Michaelis complex and confirmed the conformational movement of the thumb region owing to ligand binding. Co-crystallization of N44H with xylohexaose resulted in a hydrolyzed xylotriose bound in the active site. Co-crystallization of the wild-type enzyme with xylopentaose trapped an aglycone xylotriose and a transglycosylated glycone product. Replacing amino acids near Glu177 decreased the xylanase activity but increased the relative activity at alkaline pH. The substrate distortion in the E177Q-xylohexaose structure expands the possible conformational itinerary of this xylose ring during the enzyme-catalyzed xylan-hydrolysis reaction.
-
-	X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism.,Wan Q, Zhang Q, Hamilton-Brehm S, Weiss K, Mustyakimov M, Coates L, Langan P, Graham D, Kovalevsky A Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):11-23. doi:, 10.1107/S1399004713023626. Epub 2013 Dec 24. PMID:24419374<ref>PMID:24419374</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 4hk9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:22, 3 November 2022

OCA — Thu, 03 Nov 2022 08:22:08 GMT

←Older revision		Revision as of 08:22, 3 November 2022
Line 1:		Line 1:

	==Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)==		==Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)==
-	<StructureSection load='4hk9' size='340' side='right' caption='[[4hk9]], [[Resolution\|resolution]] 1.55Å' scene=''>	+	<StructureSection load='4hk9' size='340' side='right'caption='[[4hk9]], [[Resolution\|resolution]] 1.55Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hk9]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Atcc_13631 Atcc 13631~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HK9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hk9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trichoderma_reesei Trichoderma reesei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HK9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=~~XYP~~:~~BETA~~-D-~~XYLOPYRANOSE~~'>~~XYP~~</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PRD_900117:4beta-beta-xylotriose'>PRD_900117</scene>, <scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dfb\|2dfb]]~~, ~~[[4hk8\|4hk8]], [[4hkl\|4hkl]], [[4hko\|4hko]]~~<~~/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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [https://pdbe.org/4hk9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [https://www.ebi.ac.uk/pdbsum/4hk9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk9 ProSAT]</span></td></tr>
-	~~<tr id~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b></td><td class="sblockDat">xyn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=51453 ATCC 13631])</td></tr>~~	+
-	~~<tr id='activity~~'>~~<td class="sblockLbl"><b>Activity:~~</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [~~http~~://pdbe.org/4hk9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hk9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk9 ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/XYN2_HYPJR XYN2_HYPJR] Glycoside hydrolase involved in the hydrolysis of xylan, a major plant cell wall hemicellulose made up of 1,4-beta-linked D-xylopyranose residues. Catalyzes the endohydrolysis of the main-chain 1,4-beta-glycosidic bonds connecting the xylose subunits yielding various xylooligosaccharides and xylose (PubMed:1369024, Ref.5). The catalysis proceeds by a double-displacement reaction mechanism with a putative covalent glycosyl-enzyme intermediate, with retention of the anomeric configuration (PubMed:7988708). Produces xylobiose and xylose as the main degradation products (PubMed:19556747).<ref>PMID:1369024</ref> <ref>PMID:19556747</ref> <ref>PMID:7988708</ref> <ref>PMID:1369024</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Atcc 13631~~]]	+	[[Category: Large Structures]]
-	[[Category: ~~Endo-1,4-beta-xylanase~~]]	+	[[Category: Trichoderma reesei]]
-	[[Category: Coates, L]]	+	[[Category: Coates L]]
-	[[Category: Kovalevsky, A]]	+	[[Category: Kovalevsky A]]
-	[[Category: Langan, P]]	+	[[Category: Langan P]]
-	[[Category: Wan, Q]]	+	[[Category: Wan Q]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Induced fit mechanism]]~~	+
-	~~[[Category: Oxocarbenium ion]]~~	+
-	~~[[Category: Xylanase ii]]~~	+
-	~~[[Category: Xylohexaose]]~~	+
-	~~[[Category: Xylotriose~~]]	+

OCA at 20:26, 4 August 2016

OCA — Thu, 04 Aug 2016 20:26:39 GMT

←Older revision		Revision as of 20:26, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)==		==Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)==
	<StructureSection load='4hk9' size='340' side='right' caption='[[4hk9]], [[Resolution\|resolution]] 1.55Å' scene=''>		<StructureSection load='4hk9' size='340' side='right' caption='[[4hk9]], [[Resolution\|resolution]] 1.55Å' scene=''>
Line 7:		Line 8:
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">xyn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=51453 ATCC 13631])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">xyn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=51453 ATCC 13631])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [http://www.ebi.ac.uk/pdbsum/4hk9 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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [http://pdbe.org/4hk9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [http://www.ebi.ac.uk/pdbsum/4hk9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hk9 ProSAT]</span></td></tr>
	</table>		</table>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 17:		Line 18:
	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 4hk9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 18:13, 21 December 2014

OCA — Sun, 21 Dec 2014 18:13:57 GMT

←Older revision		Revision as of 18:13, 21 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4hk9\| PDB=4hk9 \| SCENE= }}~~	+	==Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)==
-	===Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)===	+	<StructureSection load='4hk9' size='340' side='right' caption='[[4hk9]], [[Resolution\|resolution]] 1.55Å' scene=''>
-	~~{{ABSTRACT_PUBMED_24419374}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4hk9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_13631 Atcc 13631]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HK9 FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=XYP:BETA-D-XYLOPYRANOSE'>XYP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2dfb\|2dfb]], [[4hk8\|4hk8]], [[4hkl\|4hkl]], [[4hko\|4hko]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">xyn2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=51453 ATCC 13631])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </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=4hk9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hk9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hk9 RCSB], [http://www.ebi.ac.uk/pdbsum/4hk9 PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Xylanases catalyze the hydrolysis of plant hemicellulose xylan into oligosaccharides by cleaving the main-chain glycosidic linkages connecting xylose subunits. To study ligand binding and to understand how the pH constrains the activity of the enzyme, variants of the Trichoderma reesei xylanase were designed to either abolish its activity (E177Q) or to change its pH optimum (N44H). An E177Q-xylohexaose complex structure was obtained at 1.15 A resolution which represents a pseudo-Michaelis complex and confirmed the conformational movement of the thumb region owing to ligand binding. Co-crystallization of N44H with xylohexaose resulted in a hydrolyzed xylotriose bound in the active site. Co-crystallization of the wild-type enzyme with xylopentaose trapped an aglycone xylotriose and a transglycosylated glycone product. Replacing amino acids near Glu177 decreased the xylanase activity but increased the relative activity at alkaline pH. The substrate distortion in the E177Q-xylohexaose structure expands the possible conformational itinerary of this xylose ring during the enzyme-catalyzed xylan-hydrolysis reaction.

-	~~==About this Structure==~~	+	X-ray crystallographic studies of family 11 xylanase Michaelis and product complexes: implications for the catalytic mechanism.,Wan Q, Zhang Q, Hamilton-Brehm S, Weiss K, Mustyakimov M, Coates L, Langan P, Graham D, Kovalevsky A Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):11-23. doi:, 10.1107/S1399004713023626. Epub 2013 Dec 24. PMID:24419374<ref>PMID:24419374</ref>
-	~~[[4hk9]] is a 1 chain structure. Full~~ crystallographic ~~information is available from [http~~:~~//oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4HK9 OCA]~~.	+

-	==~~Reference~~==	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~<ref group="xtra">PMID:024419374</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	</div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Atcc 13631]]
	[[Category: Endo-1,4-beta-xylanase]]		[[Category: Endo-1,4-beta-xylanase]]
-	[[Category: Coates, L.]]	+	[[Category: Coates, L]]
-	[[Category: Kovalevsky, A.]]	+	[[Category: Kovalevsky, A]]
-	[[Category: Langan, P.]]	+	[[Category: Langan, P]]
-	[[Category: Wan, Q.]]	+	[[Category: Wan, Q]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]
	[[Category: Induced fit mechanism]]		[[Category: Induced fit mechanism]]

OCA at 04:30, 13 February 2014

OCA — Thu, 13 Feb 2014 04:30:41 GMT

←Older revision		Revision as of 04:30, 13 February 2014
Line 1:		Line 1:
	{{STRUCTURE_4hk9\| PDB=4hk9 \| SCENE= }}		{{STRUCTURE_4hk9\| PDB=4hk9 \| SCENE= }}
	===Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)===		===Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)===
		+	{{ABSTRACT_PUBMED_24419374}}

	==About this Structure==		==About this Structure==
	[[4hk9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA].		[[4hk9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:024419374</ref><references group="xtra"/><references/>
	[[Category: Endo-1,4-beta-xylanase]]		[[Category: Endo-1,4-beta-xylanase]]
	[[Category: Coates, L.]]		[[Category: Coates, L.]]

OCA at 10:37, 8 January 2014

OCA — Wed, 08 Jan 2014 10:37:32 GMT

←Older revision		Revision as of 10:37, 8 January 2014
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4hk9\| PDB=4hk9 \| SCENE= }}
		+	===Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)===

-	~~The entry~~ 4hk9 is ~~ON HOLD until Jan 20 2015~~	+	==About this Structure==
-		+	[[4hk9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HK9 OCA].
-	~~Authors~~: ~~Langan, P~~.~~, Wan, Q~~.~~, Coates, L~~.~~, Kovalevsky, A~~.	+	[[Category: Endo-1,4-beta-xylanase]]
-		+	[[Category: Coates, L.]]
-	~~Description~~: ~~Crystal Structures of Mutant~~ Endo~~-beta~~-1,4-xylanase ~~II Complexed with substrate (1~~.15 A~~) and Products (1~~.~~6 A)~~	+	[[Category: Kovalevsky, A.]]
		+	[[Category: Langan, P.]]
		+	[[Category: Wan, Q.]]
		+	[[Category: Hydrolase]]
		+	[[Category: Induced fit mechanism]]
		+	[[Category: Oxocarbenium ion]]
		+	[[Category: Xylanase ii]]
		+	[[Category: Xylohexaose]]
		+	[[Category: Xylotriose]]

OCA at 09:09, 25 December 2013

OCA — Wed, 25 Dec 2013 09:09:32 GMT

←Older revision		Revision as of 09:09, 25 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hk9 is ON HOLD until ~~Dec~~ 20 ~~2014~~	+	The entry 4hk9 is ON HOLD until Jan 20 2015

	Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.		Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.

	Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)		Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)

OCA at 06:42, 6 November 2013

OCA — Wed, 06 Nov 2013 06:42:20 GMT

←Older revision		Revision as of 06:42, 6 November 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hk9 is ON HOLD until ~~Paper Publication~~	+	The entry 4hk9 is ON HOLD until Dec 20 2014

	Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.		Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.

	Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)		Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)

OCA at 10:00, 13 February 2013

OCA — Wed, 13 Feb 2013 10:00:59 GMT

←Older revision		Revision as of 10:00, 13 February 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hk9 is ON HOLD	+	The entry 4hk9 is ON HOLD until Paper Publication

	Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.		Authors: Langan, P., Wan, Q., Coates, L., Kovalevsky, A.

	Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)		Description: Crystal Structures of Mutant Endo-beta-1,4-xylanase II Complexed with substrate (1.15 A) and Products (1.6 A)

OCA: Protected "4hk9" [edit=sysop:move=sysop]

OCA — Wed, 24 Oct 2012 07:12:45 GMT

Protected "4hk9" [edit=sysop:move=sysop]

←Older revision

Revision as of 07:12, 24 October 2012