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2i16

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Revision as of 08:36, 4 July 2018

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 15K

Structural highlights

2i16 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:	1us0, 1abn, 1ads, 1az1, 1az2, 1ef3, 1el3, 1iei, 1mar, 2acq, 2acr, 2i17
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

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^[1]

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

References

↑ Petrova T, Ginell S, Mitschler A, Hazemann I, Schneider T, Cousido A, Lunin VY, Joachimiak A, Podjarny A. Ultrahigh-resolution study of protein atomic displacement parameters at cryotemperatures obtained with a helium cryostat. Acta Crystallogr D Biol Crystallogr. 2006 Dec;62(Pt 12):1535-44. Epub 2006, Nov 23. PMID:17139089 doi:10.1107/S0907444906041035

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/2i16"

@@ Line 1: / Line 1: @@
 ==Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 15K==
 <StructureSection load='2i16' size='340' side='right' caption='[[2i16]], [[Resolution|resolution]] 0.81&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1us0|1us0]], [[1abn|1abn]], [[1ads|1ads]], [[1az1|1az1]], [[1az2|1az2]], [[1ef3|1ef3]], [[1el3|1el3]], [[1iei|1iei]], [[1mar|1mar]], [[2acq|2acq]], [[2acr|2acr]], [[2i17|2i17]]</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=2i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i16 OCA], [http://pdbe.org/2i16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i16 RCSB], [http://www.ebi.ac.uk/pdbsum/2i16 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=2i16 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i16 OCA], [http://pdbe.org/2i16 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i16 RCSB], [http://www.ebi.ac.uk/pdbsum/2i16 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i16 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/i1/2i16_consurf.spt"</scriptWhenChecked>
+    <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>

2i16

From Proteopedia

Revision as of 08:36, 4 July 2018

Human aldose reductase in complex with NADP+ and the inhibitor IDD594 at temperature of 15K

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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