1n55 - Revision history

OCA at 07:52, 14 February 2024

OCA — Wed, 14 Feb 2024 07:52:51 GMT

←Older revision		Revision as of 07:52, 14 February 2024
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	<StructureSection load='1n55' size='340' side='right'caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>		<StructureSection load='1n55' size='340' side='right'caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Leime Leime~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>~~, ~~<scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</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]] 0.83Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"><~~div style~~='~~overflow~~: ~~auto; max-height: 3em;~~'>~~[[1qds\|1qds]], [[1if2\|1if2]]~~</~~div~~><~~/td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1]~~ </~~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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [https://pdbe.org/1n55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [https://www.ebi.ac.uk/pdbsum/1n55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n55 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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [https://pdbe.org/1n55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [https://www.ebi.ac.uk/pdbsum/1n55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n55 ProSAT]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/TPIS_LEIME TPIS_LEIME]
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n55 ConSurf].		</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n55 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	The atomic resolution structure of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate shows that this transition state analogue is bound in two conformations. Also for the side chain of the catalytic glutamate, Glu(167), two conformations are observed. In both conformations, a very short hydrogen bond exists between the carboxylate group of the ligand and the catalytic glutamate. The distance between O11 of PGA and Oepsilon2 of Glu(167) is 2.61 and 2.55 A for the major and minor conformations, respectively. In either conformation, Oepsilon1 of Glu(167) is hydrogen-bonded to a water network connecting the side chain with bulk solvent. This network also occurs in two mutually exclusive arrangements. Despite the structural disorder in the active site, the C termini of the beta strands that construct the active site display the least anisotropy compared with the rest of the protein. The loops following these beta strands display various degrees of anisotropy, with the tip of the dimer interface loop 3 having very low anisotropy and the C-terminal region of the active site loop 6 having the highest anisotropy. The pyrrolidine ring of Pro(168) at the N-terminal region of loop 6 is in a strained planar conformation to facilitate loop opening and product release.
-
-	Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.,Kursula I, Wierenga RK J Biol Chem. 2003 Mar 14;278(11):9544-51. Epub 2003 Jan 9. PMID:12522213<ref>PMID:12522213</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 1n55" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
	*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]		*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: ~~Leime]]~~	+	[[Category: Leishmania mexicana]]
-	~~[[Category: Triose-phosphate isomerase~~]]	+	[[Category: Kursula I]]
-	[[Category: Kursula, I]]	+	[[Category: Wierenga RK]]
-	[[Category: Wierenga~~, R K]]~~	+
-	~~[[Category: Atomic resolution]]~~	+
-	~~[[Category: Enzyme-ligand complex]]~~	+
-	~~[[Category: Isomerase]]~~	+
-	~~[[Category: Low-barrier hydrogen bond]]~~	+
-	~~[[Category: Tim]]~~	+
-	~~[[Category: Transition-state analogue~~]]	+

OCA at 09:32, 5 May 2021

OCA — Wed, 05 May 2021 09:32:34 GMT

←Older revision		Revision as of 09:32, 5 May 2021
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	<StructureSection load='1n55' size='340' side='right'caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>		<StructureSection load='1n55' size='340' side='right'caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1N55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qds\|1qds]], [[1if2\|1if2]]</div></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [~~http~~://pdbe.org/1n55 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1n55 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1n55 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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [https://pdbe.org/1n55 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [https://www.ebi.ac.uk/pdbsum/1n55 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n55 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
Line 30:		Line 30:

	==See Also==		==See Also==
-	*[[Triose ~~Phosphate Isomerase~~\|Triose ~~Phosphate Isomerase~~]]	+	*[[Triose phosphate isomerase 3D structures\|Triose phosphate isomerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 08:03, 31 July 2019

OCA — Wed, 31 Jul 2019 08:03:04 GMT

←Older revision		Revision as of 08:03, 31 July 2019
Line 1:		Line 1:

	==0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate==		==0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate==
-	<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>	+	<StructureSection load='1n55' size='340' side='right'caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
Line 13:		Line 13:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n55_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n55_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 35:		Line 35:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Large Structures]]
	[[Category: Leime]]		[[Category: Leime]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]

OCA at 10:23, 25 October 2017

OCA — Wed, 25 Oct 2017 10:23:57 GMT

←Older revision		Revision as of 10:23, 25 October 2017
Line 1:		Line 1:
		+
	==0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate==		==0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate==
	<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>		<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://pdbe.org/1n55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://pdbe.org/1n55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1n55 ProSAT]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n55 ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">

OCA at 17:13, 11 September 2015

OCA — Fri, 11 Sep 2015 17:13:37 GMT

←Older revision		Revision as of 17:13, 11 September 2015
Line 2:		Line 2:
	<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>		<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Leishmania_mexicana Leishmania mexicana~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leime Leime]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://pdbe.org/1n55 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 PDBsum]</span></td></tr>
	</table>		</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
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	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 1n55" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 33:		Line 34:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Leishmania mexicana~~]]	+	[[Category: Leime]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
	[[Category: Kursula, I]]		[[Category: Kursula, I]]

OCA at 16:14, 5 January 2015

OCA — Mon, 05 Jan 2015 16:14:42 GMT

OCA at 14:19, 29 September 2014

OCA — Mon, 29 Sep 2014 14:19:55 GMT

←Older revision		Revision as of 14:19, 29 September 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1n55\| PDB=1n55 \| SCENE= }}~~	+	==0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate==
-	===0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate===	+	<StructureSection load='1n55' size='340' side='right' caption='[[1n55]], [[Resolution\|resolution]] 0.83Å' scene=''>
-	~~{{ABSTRACT_PUBMED_12522213}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 PDBsum]</span></td></tr>
		+	<table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n5/1n55_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The atomic resolution structure of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate shows that this transition state analogue is bound in two conformations. Also for the side chain of the catalytic glutamate, Glu(167), two conformations are observed. In both conformations, a very short hydrogen bond exists between the carboxylate group of the ligand and the catalytic glutamate. The distance between O11 of PGA and Oepsilon2 of Glu(167) is 2.61 and 2.55 A for the major and minor conformations, respectively. In either conformation, Oepsilon1 of Glu(167) is hydrogen-bonded to a water network connecting the side chain with bulk solvent. This network also occurs in two mutually exclusive arrangements. Despite the structural disorder in the active site, the C termini of the beta strands that construct the active site display the least anisotropy compared with the rest of the protein. The loops following these beta strands display various degrees of anisotropy, with the tip of the dimer interface loop 3 having very low anisotropy and the C-terminal region of the active site loop 6 having the highest anisotropy. The pyrrolidine ring of Pro(168) at the N-terminal region of loop 6 is in a strained planar conformation to facilitate loop opening and product release.

-	~~==About this Structure==~~	+	Crystal structure of triosephosphate isomerase complexed with 2-phosphoglycolate at 0.83-A resolution.,Kursula I, Wierenga RK J Biol Chem. 2003 Mar 14;278(11):9544-51. Epub 2003 Jan 9. PMID:12522213<ref>PMID:12522213</ref>
-	~~[[1n55]] is a 1 chain~~ structure with ~~sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Leishmania_mexicana Leishmania mexicana]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=1N55 OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]		*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:012522213<~~/~~ref~~><~~ref group="xtra">PMID:018754631</ref><references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Leishmania mexicana]]		[[Category: Leishmania mexicana]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]

OCA at 09:37, 11 March 2013

OCA — Mon, 11 Mar 2013 09:37:18 GMT

←Older revision		Revision as of 09:37, 11 March 2013
Line 1:		Line 1:
-	[[Image:1n55.png\|left\|200px]]
-
	{{STRUCTURE_1n55\| PDB=1n55 \| SCENE= }}		{{STRUCTURE_1n55\| PDB=1n55 \| SCENE= }}
-
	===0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate===		===0.83A resolution structure of the E65Q mutant of Leishmania mexicana triosephosphate isomerase complexed with 2-phosphoglycolate===
-
	{{ABSTRACT_PUBMED_12522213}}		{{ABSTRACT_PUBMED_12522213}}

OCA at 20:32, 20 October 2012

OCA — Sat, 20 Oct 2012 20:32:29 GMT

←Older revision		Revision as of 20:32, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1n55]] is a 1 chain structure ~~of [[Triose Phosphate Isomerase]]~~ with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA].	+	[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA].

	==See Also==		==See Also==

OCA at 02:48, 29 August 2012

OCA — Wed, 29 Aug 2012 02:48:50 GMT

←Older revision		Revision as of 02:48, 29 August 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[1n55]] is a 1 chain structure of ~~[[TIM test]] and~~ [[Triose Phosphate Isomerase]] with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA].	+	[[1n55]] is a 1 chain structure of [[Triose Phosphate Isomerase]] with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA].

	==See Also==		==See Also==
-	*[[TIM test\|TIM test]]
	*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]		*[[Triose Phosphate Isomerase\|Triose Phosphate Isomerase]]

←Older revision		Revision as of 16:14, 5 January 2015
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>		<table><tr><td colspan='2'>[[1n55]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Leishmania_mexicana Leishmania mexicana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N55 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N55 FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PGA:2-PHOSPHOGLYCOLIC+ACID'>PGA</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1qds\|1qds]], [[1if2\|1if2]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Triose-phosphate_isomerase Triose-phosphate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.1 5.3.1.1] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 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=1n55 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n55 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n55 RCSB], [http://www.ebi.ac.uk/pdbsum/1n55 PDBsum]</span></td></tr>
-	<table>	+	</table>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 35:		Line 35:
	[[Category: Leishmania mexicana]]		[[Category: Leishmania mexicana]]
	[[Category: Triose-phosphate isomerase]]		[[Category: Triose-phosphate isomerase]]
-	[[Category: Kursula, I.]]	+	[[Category: Kursula, I]]
-	[[Category: Wierenga, R K.]]	+	[[Category: Wierenga, R K]]
	[[Category: Atomic resolution]]		[[Category: Atomic resolution]]
	[[Category: Enzyme-ligand complex]]		[[Category: Enzyme-ligand complex]]