1el3

From Proteopedia

(Difference between revisions)

Revision as of 09:38, 21 July 2021

HUMAN ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR

Structural highlights

1el3 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Activity:	Aldehyde reductase, with EC number 1.1.1.21
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystallographic structure of the complex between human aldose reductase (AR2) and one of its inhibitors, IDD384, has been solved at 1.7 A resolution from crystals obtained at pH 5.0. This structure shows that the binding of the inhibitor's hydrophilic head to the catalytic residues Tyr48 and His110 differs from that found previously with porcine AR2. The difference is attributed to a change in the protonation state of the inhibitor (pK(a) = 4.52) when soaked with crystals of human (at pH 5.0) or pig lens AR2 (at pH 6.2). This work demonstrates how strongly the detailed binding of the inhibitor's polar head depends on its protonation state.

The structure of human aldose reductase bound to the inhibitor IDD384.,Calderone V, Chevrier B, Van Zandt M, Lamour V, Howard E, Poterszman A, Barth P, Mitschler A, Lu J, Dvornik DM, Klebe G, Kraemer O, Moorman AR, Moras D, Podjarny A Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):536-40. PMID:10771421^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Calderone V, Chevrier B, Van Zandt M, Lamour V, Howard E, Poterszman A, Barth P, Mitschler A, Lu J, Dvornik DM, Klebe G, Kraemer O, Moorman AR, Moras D, Podjarny A. The structure of human aldose reductase bound to the inhibitor IDD384. Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):536-40. PMID:10771421

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1el3"

@@ Line 3: / Line 3: @@
 <StructureSection load='1el3' size='340' side='right'caption='[[1el3]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1el3]] 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=1EL3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EL3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1el3]] 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=1EL3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EL3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=I84:[2,6-DIMETHYL-4-(2-O-TOLYL-ACETYLAMINO)-BENZENESULFONYL]-GLYCINE'>I84</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=I84:[2,6-DIMETHYL-4-(2-O-TOLYL-ACETYLAMINO)-BENZENESULFONYL]-GLYCINE'>I84</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></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=1el3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el3 OCA], [http://pdbe.org/1el3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1el3 RCSB], [http://www.ebi.ac.uk/pdbsum/1el3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1el3 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=1el3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1el3 OCA], [https://pdbe.org/1el3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1el3 RCSB], [https://www.ebi.ac.uk/pdbsum/1el3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1el3 ProSAT]</span></td></tr>
 </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.
+[[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1el3

From Proteopedia

Revision as of 09:38, 21 July 2021

HUMAN ALDOSE REDUCTASE COMPLEXED WITH IDD384 INHIBITOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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