This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

3bcj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:10, 31 October 2018

Crystal structure of Aldose Reductase complexed with 2S4R (Stereoisomer of Fidarestat, 2S4S) at 0.78 A

Structural highlights

3bcj 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:	, ,
Related:	1x98, 1pwm
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 structure of human aldose reductase in complex with the 2 S4 R stereoisomer of the potent inhibitor Fidarestat ((2 S,4 S)-6-fluoro-2',5'-dioxospiro-[chroman-4,4'-imidazoline]-2-carboxamide) was determined at 15 K and a resolution of 0.78 A. The structure of the complex provides experimental evidence for the inhibition mechanism in which Fidarestat is initially bound neutral and then becomes negatively charged by donating the proton at the 1'-position nitrogen of the cyclic imide ring to the N2 atom of the catalytic His110.

Unusual Binding Mode of the 2S4R Stereoisomer of the Potent Aldose Reductase Cyclic Imide Inhibitor Fidarestat (2S4S) in the 15 K Crystal Structure of the Ternary Complex Refined at 0.78 A Resolution: Implications for the Inhibition Mechanism.,Zhao HT, Hazemann I, Mitschler A, Carbone V, Joachimiak A, Ginell S, Podjarny A, El-Kabbani O J Med Chem. 2008 Mar 13;51(5):1478-1481. Epub 2008 Feb 20. PMID:18284183^[1]

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

References

↑ Zhao HT, Hazemann I, Mitschler A, Carbone V, Joachimiak A, Ginell S, Podjarny A, El-Kabbani O. Unusual Binding Mode of the 2S4R Stereoisomer of the Potent Aldose Reductase Cyclic Imide Inhibitor Fidarestat (2S4S) in the 15 K Crystal Structure of the Ternary Complex Refined at 0.78 A Resolution: Implications for the Inhibition Mechanism. J Med Chem. 2008 Mar 13;51(5):1478-1481. Epub 2008 Feb 20. PMID:18284183 doi:10.1021/jm701514k

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/3bcj"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Aldose Reductase complexed with 2S4R (Stereoisomer of Fidarestat, 2S4S) at 0.78 A==
 <StructureSection load='3bcj' size='340' side='right' caption='[[3bcj]], [[Resolution|resolution]] 0.78&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1x98|1x98]], [[1pwm|1pwm]]</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=3bcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcj OCA], [http://pdbe.org/3bcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bcj RCSB], [http://www.ebi.ac.uk/pdbsum/3bcj 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=3bcj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bcj OCA], [http://pdbe.org/3bcj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bcj RCSB], [http://www.ebi.ac.uk/pdbsum/3bcj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bcj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 14: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/3bcj_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bc/3bcj_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 40: / Line 41: @@
 [[Category: El-Kabbani, O]]
 [[Category: Zhao, H T]]
+[[Category: Acetylation]]
 [[Category: Aldo-keto reductase]]
 [[Category: Cataract]]
+[[Category: Cytoplasm]]
 [[Category: Diabetes]]
 [[Category: Drug design]]
@@ Line 47: / Line 50: @@
 [[Category: Oxidoreductase]]
 [[Category: Polyl pathway]]
+[[Category: Polymorphism]]

3bcj

From Proteopedia

Revision as of 08:10, 31 October 2018

Crystal structure of Aldose Reductase complexed with 2S4R (Stereoisomer of Fidarestat, 2S4S) at 0.78 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox