2i17

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[[Image:2i17.png|left|200px]]
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==Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K==
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<StructureSection load='2i17' size='340' side='right' caption='[[2i17]], [[Resolution|resolution]] 0.81&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2i17]] 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=2I17 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I17 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=LDT:IDD594'>LDT</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene><br>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us0|1us0]], [[2i16|2i16]], [[1ads|1ads]], [[1az1|1az1]], [[1az2|1az2]], [[1ef3|1ef3]], [[1el3|1el3]], [[1iei|1iei]], [[1mar|1mar]], [[2acq|2acq]]</td></tr>
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<tr><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>
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<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=2i17 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i17 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i17 RCSB], [http://www.ebi.ac.uk/pdbsum/2i17 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/i1/2i17_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Two X-ray data sets for a complex of human aldose reductase (h-AR) with the inhibitor IDD 594 and the cofactor NADP(+) were collected from two different parts of the same crystal to a resolution of 0.81 A at 15 and 60 K using cold helium gas as cryogen. The contribution of temperature to the atomic B values was estimated by comparison of the independently refined models. It was found that although being slightly different for different kinds of atoms, the differences (deltaB) in the isotropic equivalents B of atomic displacement parameters (ADPs) were approximately constant (about 1.7 A(2)) for well ordered atoms as the temperature was increased from 15 to 60 K. The mean value of this difference varied according to the number of non-H atoms covalently bound to the parent atom. Atoms having a B value of higher than 8 A(2) at 15 K showed much larger deviations of deltaB from the average value, which might reflect partial occupancy of atomic sites. An analysis of the anisotropy of ADPs for individual atoms revealed an increase in the isotropy of ADPs with the increase of the temperature from 15 to 60 K. In a separate experiment, a 0.93 A resolution data set was collected from a different crystal of the same complex at 100 K using cold nitrogen as a cryogen. The effects of various errors on the atomic B values were estimated by comparison of the refined models and the temperature-dependent component was inferred. It was found that both decreasing the data redundancy and increasing the resolution cutoff led to an approximately constant increase in atomic B values for well ordered atoms.
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{{STRUCTURE_2i17| PDB=2i17 | SCENE= }}
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Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat.,Petrova T, Ginell S, Mitschler A, Hazemann I, Schneider T, Cousido A, Lunin VY, Joachimiak A, Podjarny A Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1535-44. Epub 2006, Nov 23. PMID:17139089<ref>PMID:17139089</ref>
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===Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_17139089}}
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==About this Structure==
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[[2i17]] 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=2I17 OCA].
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==See Also==
==See Also==
*[[Aldose Reductase|Aldose Reductase]]
*[[Aldose Reductase|Aldose Reductase]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:017139089</ref><references group="xtra"/>
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__TOC__
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</StructureSection>
[[Category: Aldehyde reductase]]
[[Category: Aldehyde reductase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 05:45, 29 September 2014

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 60K

2i17, resolution 0.81Å

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