2i16: Difference between revisions
New page: left|200px<br /> <applet load="2i16" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i16, resolution 0.81Å" /> '''Human aldose reduct... |
No edit summary |
||
| (16 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
== | ==Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 15K== | ||
Two X-ray data sets for a complex of human aldose reductase (h-AR) with | <StructureSection load='2i16' size='340' side='right'caption='[[2i16]], [[Resolution|resolution]] 0.81Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2i16]] 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=2I16 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I16 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 0.81Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></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=2i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i16 OCA], [https://pdbe.org/2i16 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i16 RCSB], [https://www.ebi.ac.uk/pdbsum/2i16 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i16 ProSAT]</span></td></tr> | |||
</table> | |||
== 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. | |||
== 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/i1/2i16_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/main_output.php?pdb_ID=2i16 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[ | <div class="pdbe-citations 2i16" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cousido | [[Category: Cousido A]] | ||
[[Category: Ginell | [[Category: Ginell S]] | ||
[[Category: Hasemann | [[Category: Hasemann I]] | ||
[[Category: Joachimiak | [[Category: Joachimiak A]] | ||
[[Category: Lunin | [[Category: Lunin VY]] | ||
[[Category: Mitshler | [[Category: Mitshler A]] | ||
[[Category: Petrova | [[Category: Petrova T]] | ||
[[Category: Podjarny | [[Category: Podjarny A]] | ||
[[Category: Schneider | [[Category: Schneider T]] | ||
