3lqg - Revision history

OCA at 08:46, 7 February 2024

OCA — Wed, 07 Feb 2024 08:46:54 GMT

←Older revision		Revision as of 08:46, 7 February 2024
Line 3:		Line 3:
	<StructureSection load='3lqg' size='340' side='right'caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='3lqg' size='340' side='right'caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 1.35Å</td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</div></td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [https://pdbe.org/3lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [https://www.ebi.ac.uk/pdbsum/3lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqg 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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [https://pdbe.org/3lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [https://www.ebi.ac.uk/pdbsum/3lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.	+	[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Improvements on the computational methods for affinity prediction from the structure of protein-ligand complexes require a better understanding of the nature of molecular interactions and biomolecular recognition principles. In the present contribution, the binding of two chemically closely related human aldose reductase inhibitors had been studied by high-resolution X-ray analysis (0.92-1.35 A) and isothermal titration calorimetry against a series of single-site mutants of the wild-type protein. A crucial threonine thought to be involved in a short bromine-to-oxygen halogen bond to the inhibitors in the wild type has been mutated to the structurally similar residues alanine, cysteine, serine and valine. Overall, structurally, the binding mode of the inhibitors is conserved; however, small but significant geometrical adaptations are observed as a consequence of the spatial and electronic changes at the mutation site. They involve the opening of a central bond angle and shifts in consequence of the lost or gained halogen bonds. Remarkably, the tiny structural changes are responded by partly strong modulation of the thermodynamic profiles. Even though the free energy of binding is maximally perturbed by only 7 kJ/mol, much stronger modulations and shifts in the enthalpy and entropy signatures are revealed, which indicate a pronounced enthalpy/entropy compensation. However, an explanatory correlation can be detected when facing these perturbances against the small structural changes. This also provides deeper insights into how single-site mutations can alter the selectivity profile of closely related ligands against a target protein.	+
-		+
-	Tracing the detail: how mutations affect binding modes and thermodynamic signatures of closely related aldose reductase inhibitors.,Koch C, Heine A, Klebe G J Mol Biol. 2011 Mar 11;406(5):700-12. Epub 2010 Dec 23. PMID:21185307<ref>PMID:21185307</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3lqg" style="background-color:#fffaf0;"></div>~~	+

	==See Also==		==See Also==
	*[[Aldose reductase 3D structures\|Aldose reductase 3D structures]]		*[[Aldose reductase 3D structures\|Aldose reductase 3D structures]]
-	== References ==
-	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aldehyde reductase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Heine, A]]	+	[[Category: Heine A]]
-	[[Category: Klebe, G]]	+	[[Category: Klebe G]]
-	[[Category: Koch, C]]	+	[[Category: Koch C]]
-	~~[[Category: Nadp]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]~~	+
-	~~[[Category: Phosphoprotein]]~~	+
-	~~[[Category: T113a mutant~~]]	+

OCA at 13:42, 4 May 2022

OCA — Wed, 04 May 2022 13:42:05 GMT

←Older revision		Revision as of 13:42, 4 May 2022
Line 1:		Line 1:

	==Human aldose reductase mutant T113A complexed with IDD388==		==Human aldose reductase mutant T113A complexed with IDD388==
-	<StructureSection load='3lqg' size='340' side='right' caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>	+	<StructureSection load='3lqg' size='340' side='right'caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3LQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LQG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [~~http~~://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [~~http~~://pdbe.org/3lqg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3lqg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqg 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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [https://pdbe.org/3lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [https://www.ebi.ac.uk/pdbsum/3lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.	+	[[https://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:

	==See Also==		==See Also==
-	*[[Aldose ~~Reductase~~\|Aldose ~~Reductase~~]]	+	*[[Aldose reductase 3D structures\|Aldose reductase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
Line 30:		Line 30:
	[[Category: Aldehyde reductase]]		[[Category: Aldehyde reductase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
	[[Category: Klebe, G]]		[[Category: Klebe, G]]

OCA at 22:16, 4 August 2016

OCA — Thu, 04 Aug 2016 22:16:30 GMT

←Older revision		Revision as of 22:16, 4 August 2016
Line 1:		Line 1:
		+
	==Human aldose reductase mutant T113A complexed with IDD388==		==Human aldose reductase mutant T113A complexed with IDD388==
	<StructureSection load='3lqg' size='340' side='right' caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>		<StructureSection load='3lqg' size='340' side='right' caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [http://www.ebi.ac.uk/pdbsum/3lqg 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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [http://pdbe.org/3lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [http://www.ebi.ac.uk/pdbsum/3lqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3lqg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 3lqg" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 27:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Aldehyde reductase]]		[[Category: Aldehyde reductase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Heine, A]]		[[Category: Heine, A]]
	[[Category: Klebe, G]]		[[Category: Klebe, G]]

OCA at 13:35, 25 December 2014

OCA — Thu, 25 Dec 2014 13:35:23 GMT

←Older revision		Revision as of 13:35, 25 December 2014
Line 9:		Line 9:
	<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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [http://www.ebi.ac.uk/pdbsum/3lqg 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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [http://www.ebi.ac.uk/pdbsum/3lqg PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/ALDR_HUMAN ALDR_HUMAN]] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 09:48, 9 December 2014

OCA — Tue, 09 Dec 2014 09:48:06 GMT

←Older revision		Revision as of 09:48, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3lqg.~~png~~\|~~left~~\|~~200px~~]]	+	==Human aldose reductase mutant T113A complexed with IDD388==
		+	<StructureSection load='3lqg' size='340' side='right' caption='[[3lqg]], [[Resolution\|resolution]] 1.35Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3lqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LQG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=388:(2-{[(4-BROMO-2-FLUOROBENZYL)AMINO]CARBONYL}-5-CHLOROPHENOXY)ACETIC+ACID'>388</scene>, <scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3lep\|3lep]], [[2iki\|2iki]], [[1us0\|1us0]], [[3lql\|3lql]], [[3lbo\|3lbo]], [[3ld5\|3ld5]], [[3lz3\|3lz3]], [[3m4h\|3m4h]], [[3lz5\|3lz5]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">alr2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Aldehyde_reductase Aldehyde reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.21 1.1.1.21] </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=3lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3lqg RCSB], [http://www.ebi.ac.uk/pdbsum/3lqg PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Improvements on the computational methods for affinity prediction from the structure of protein-ligand complexes require a better understanding of the nature of molecular interactions and biomolecular recognition principles. In the present contribution, the binding of two chemically closely related human aldose reductase inhibitors had been studied by high-resolution X-ray analysis (0.92-1.35 A) and isothermal titration calorimetry against a series of single-site mutants of the wild-type protein. A crucial threonine thought to be involved in a short bromine-to-oxygen halogen bond to the inhibitors in the wild type has been mutated to the structurally similar residues alanine, cysteine, serine and valine. Overall, structurally, the binding mode of the inhibitors is conserved; however, small but significant geometrical adaptations are observed as a consequence of the spatial and electronic changes at the mutation site. They involve the opening of a central bond angle and shifts in consequence of the lost or gained halogen bonds. Remarkably, the tiny structural changes are responded by partly strong modulation of the thermodynamic profiles. Even though the free energy of binding is maximally perturbed by only 7 kJ/mol, much stronger modulations and shifts in the enthalpy and entropy signatures are revealed, which indicate a pronounced enthalpy/entropy compensation. However, an explanatory correlation can be detected when facing these perturbances against the small structural changes. This also provides deeper insights into how single-site mutations can alter the selectivity profile of closely related ligands against a target protein.

-	~~{{STRUCTURE_3lqg\| PDB=3lqg \| SCENE= }}~~	+	Tracing the detail: how mutations affect binding modes and thermodynamic signatures of closely related aldose reductase inhibitors.,Koch C, Heine A, Klebe G J Mol Biol. 2011 Mar 11;406(5):700-12. Epub 2010 Dec 23. PMID:21185307<ref>PMID:21185307</ref>

-	~~===Human aldose reductase mutant T113A complexed with IDD388===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21185307}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3lqg]] is~~ a ~~1 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].~~	+

	==See Also==		==See Also==
	*[[Aldose Reductase\|Aldose Reductase]]		*[[Aldose Reductase\|Aldose Reductase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021185307<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Aldehyde reductase]]		[[Category: Aldehyde reductase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Heine, A.]]	+	[[Category: Heine, A]]
-	[[Category: Klebe, G.]]	+	[[Category: Klebe, G]]
-	[[Category: Koch, C.]]	+	[[Category: Koch, C]]
	[[Category: Nadp]]		[[Category: Nadp]]
	[[Category: Oxidoreductase]]		[[Category: Oxidoreductase]]

OCA at 17:18, 20 October 2012

OCA — Sat, 20 Oct 2012 17:18:26 GMT

←Older revision		Revision as of 17:18, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3lqg]] is a 1 chain structure ~~of [[Aldose Reductase]]~~ with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].	+	[[3lqg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].

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

OCA at 00:28, 27 July 2012

OCA — Fri, 27 Jul 2012 00:28:31 GMT

←Older revision		Revision as of 00:28, 27 July 2012
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	[[Image:3lqg.png\|left\|200px]]		[[Image:3lqg.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3lqg\| PDB=3lqg \| SCENE= }}		{{STRUCTURE_3lqg\| PDB=3lqg \| SCENE= }}

	===Human aldose reductase mutant T113A complexed with IDD388===		===Human aldose reductase mutant T113A complexed with IDD388===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21185307}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21185307 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_21185307}}		{{ABSTRACT_PUBMED_21185307}}

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	==See Also==		==See Also==
-	*[[Aldose Reductase]]	+	*[[Aldose Reductase\|Aldose Reductase]]

	==Reference==		==Reference==

OCA: Protected "3lqg" [edit=sysop:move=sysop]

OCA — Wed, 24 Aug 2011 06:29:16 GMT

Protected "3lqg" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:29, 24 August 2011

OCA at 06:29, 24 August 2011

OCA — Wed, 24 Aug 2011 06:29:13 GMT

←Older revision		Revision as of 06:29, 24 August 2011
Line 1:		Line 1:
-	~~{{Seed}}~~	+	[[Image:3lqg.png\|left\|200px]]
-	[[Image:3lqg.~~jpg~~\|left\|200px]]	+

	<!--		<!--
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	===Human aldose reductase mutant T113A complexed with IDD388===		===Human aldose reductase mutant T113A complexed with IDD388===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21185307}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21185307 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21185307}}

	==About this Structure==		==About this Structure==
-	~~3LQG~~ is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].	+	[[3lqg]] is a 1 chain structure of [[Aldose Reductase]] with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].
		+
		+	==See Also==
		+	*[[Aldose Reductase]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:021185307</ref><references group="xtra"/>
	[[Category: Aldehyde reductase]]		[[Category: Aldehyde reductase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
Line 25:		Line 36:
	[[Category: Phosphoprotein]]		[[Category: Phosphoprotein]]
	[[Category: T113a mutant]]		[[Category: T113a mutant]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:41:27 2010''

OCA at 05:29, 15 December 2010

OCA — Wed, 15 Dec 2010 05:29:08 GMT

←Older revision		Revision as of 05:29, 15 December 2010
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{Seed}}
		+	[[Image:3lqg.jpg\|left\|200px]]

-	The ~~entry 3lqg~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3lqg", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3lqg\| PDB=3lqg \| SCENE= }}

-	~~Authors: Koch, C., Heine, A., Klebe, G.~~	+	===Human aldose reductase mutant T113A complexed with IDD388===

-	Description: Human aldose reductase mutant T113A complexed with IDD388

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Mar 10 13~~:14:02 2010''	+	==About this Structure==
		+	3LQG is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LQG OCA].
		+	[[Category: Aldehyde reductase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Heine, A.]]
		+	[[Category: Klebe, G.]]
		+	[[Category: Koch, C.]]
		+	[[Category: Nadp]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
		+	[[Category: Phosphoprotein]]
		+	[[Category: T113a mutant]]
		+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 15 08:41:27 2010''