Aldo-keto reductase
From Proteopedia
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</StructureSection> | </StructureSection> | ||
| - | ==3D structures of aldo-keto reductase== | ||
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| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
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| - | *AKR1B1 | ||
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| - | **[[2j8t]] – hAKR1B1 + NADP - human<br /> | ||
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| - | *AKR1B4 | ||
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| - | **[[4hbk]] – AKR1B4 – blood fluke<br /> | ||
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| - | *AKR1B10 | ||
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| - | **[[4xzm]], [[4gqg]] – hAKR1B10 + NADP <br /> | ||
| - | **[[4xzn]] – hAKR1B10 (mutant) + NADP <br /> | ||
| - | **[[4jih]], [[4jii]], [[4i5x]], [[5y7n]] – hAKR1B10 + NADP + inhibitor <br /> | ||
| - | **[[4ga8]], [[4gab]], [[1zua]], [[5liy]], [[5lik]], [[5liu]], [[5liw]], [[5lix]], [[4xzl]], [[4wev]], [[4icc]], [[5m2f]] – hAKR1B10 (mutant) + NADP + inhibitor <br /> | ||
| - | **[[4gq0]] – hAKR1B10 + NADP + caffeic acid ester<br /> | ||
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| - | *AKR1B14 | ||
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| - | **[[3o3r]] – rAKR1B14 + NADP - rat<br /> | ||
| - | **[[3qkz]] – rAKR1B14 (mutant) + NADP <br /> | ||
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| - | *AKR1C1 See [[Hydroxysteroid dehydrogenase]] 20-alpha HSD | ||
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| - | *AKR1C2 or 3-alpha hydroxysteroid dehydrogenase See [[Hydroxysteroid dehydrogenase]] 3-alpha HSD | ||
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| - | *AKR1C3 See [[Prostaglandin F synthase]] | ||
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| - | *AKR1C4 | ||
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| - | **[[2fvl]] – hAKR1C4 + NADP <br /> | ||
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| - | *AKR1C13 | ||
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| - | **[[6m7k]] – AKR1C13 + cyclic AMP-AMP-GMP - mouse<br /> | ||
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| - | *AKR1C21 or 17-alpha hydroxysteroid dehydrogenase See [[Hydroxysteroid dehydrogenase]] 17-alpha HSD | ||
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| - | *AKR1D1 or 3-oxo-5-beta-steroid 4-dehydrogenase | ||
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| - | **[[3caq]], [[3buv]], [[3bv7]] – hAKR1D1 + NADP <br /> | ||
| - | **[[3dop]] – hAKR1D1 + NADP + 5-beta-dehydrotestosterone<br /> | ||
| - | **[[3uzy]] – hAKR1D1 (mutant) + NADP + 5-beta-dehydrotestosterone<br /> | ||
| - | **[[3bur]] – hAKR1D1 (mutant) + NADP + testosterone<br /> | ||
| - | **[[3uzz]] – hAKR1D1 (mutant) + NADP + 5-delta-androstenedione<br /> | ||
| - | **[[3cas]] – hAKR1D1 + NADP + 4-androstenedione<br /> | ||
| - | **[[3g1r]] – hAKR1D1 + NADP + finasteride<br /> | ||
| - | **[[3cav]] – hAKR1D1 + NADP + 5-beta-pregnan-3,20-dione<br /> | ||
| - | **[[3cmf]] – hAKR1D1 + NADP + cortisone<br /> | ||
| - | **[[3cot]] – hAKR1D1 + NADP + progesterone<br /> | ||
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| - | *AKR2E4 | ||
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| - | **[[3wcz]] – AKR2E4 + NADP – silk moth<br /> | ||
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| - | *AKR4C8 | ||
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| - | **[[3h7r]] – AtAKR4C8 + NADP – ''Arabidopsis thaliana''<br /> | ||
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| - | *AKR4C9 | ||
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| - | **[[3h7u]] – AtAKR4C8 + NADP <br /> | ||
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| - | *AKR4C13 See [[Aldose Reductase]] | ||
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| - | *AKR7A1 or aflatoxin aldehyde reductase | ||
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| - | **[[1gve]] – AKR7A1 + NADP – rat<br /> | ||
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| - | *AKR11A or IOLS protein | ||
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| - | **[[1pyf]] – BsAKR11A – ''Bacillus subtilis'' <br /> | ||
| - | **[[1pz0]] – BsAKR11A + NADP <br /> | ||
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| - | *AKR11B or general stress protein 69 | ||
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| - | **[[1pz1]] – BsAKR11B + NADP <br /> | ||
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| - | *AKR11B4 | ||
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| - | **[[3n2t]] – AKR11B4 – ''Gluconobacter oxydans'' <br /> | ||
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| - | *AKR11C1 | ||
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| - | **[[1ynp]] – BhAKR11C1 – ''Bacillus halodurans'' <br /> | ||
| - | **[[1ynq]] – BhAKR11C1 + NADP <br /> | ||
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| - | *AKR14A1 | ||
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| - | **[[4ast]] – EcAKR14A1 – ''Escherichia coli''<br /> | ||
| - | **[[4aub]] – EcAKR14A1 + NADP <br /> | ||
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| - | *AKR | ||
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| - | **[[4xap]] – RmAKR – ''Rhizobium meliloti''<br /> | ||
| - | **[[5c7h]] – RmAKR + NADP <br /> | ||
| - | **[[4xk2]] – AKR – ''Polaromonas''<br /> | ||
| - | **[[6cia]] – KpAKR + NADP – Klebsiella pneumoniae<br /> | ||
| - | **[[4wgh]] – AKR (mutant) + NADP <br /> | ||
| - | **[[3n6q]] – EcAKR <br /> | ||
| - | **[[3o0k]] – AKR – ''Brucella melitensis''<br /> | ||
| - | **[[2wzt]] – MsAKR – ''Mycobacterium smegmatis''<br /> | ||
| - | **[[2wzm]] – MsAKR + ligand<br /> | ||
| - | **[[5t79]] – AKR + NADP – ''Salmonella typhimurium''<br /> | ||
| - | **[[5ket]] – AKR1 + NADP – ''Coptotermes gestroi''<br /> | ||
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| - | }} | ||
Revision as of 10:30, 4 March 2019
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References
- ↑ Penning TM. The aldo-keto reductases (AKRs): Overview. Chem Biol Interact. 2015 Jun 5;234:236-46. doi: 10.1016/j.cbi.2014.09.024. Epub, 2014 Oct 7. PMID:25304492 doi:http://dx.doi.org/10.1016/j.cbi.2014.09.024
- ↑ Drury JE, Mindnich R, Penning TM. Characterization of disease-related 5beta-reductase (AKR1D1) mutations reveals their potential to cause bile acid deficiency. J Biol Chem. 2010 Aug 6;285(32):24529-37. doi: 10.1074/jbc.M110.127779. Epub 2010, Jun 3. PMID:20522910 doi:http://dx.doi.org/10.1074/jbc.M110.127779
- ↑ Cousido-Siah A, Ruiz FX, Mitschler A, Porte S, de Lera AR, Martin MJ, Manzanaro S, de la Fuente JA, Terwesten F, Betz M, Klebe G, Farres J, Pares X, Podjarny A. Identification of a novel polyfluorinated compound as a lead to inhibit the human enzymes aldose reductase and AKR1B10: structure determination of both ternary complexes and implications for drug design. Acta Crystallogr D Biol Crystallogr. 2014 Mar;70(Pt 3):889-903. doi:, 10.1107/S1399004713033452. Epub 2014 Feb 27. PMID:24598757 doi:http://dx.doi.org/10.1107/S1399004713033452
