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TitleHuman prostaglandin/alkenal reductases: substrate specificities, inhibitor profiles, structural insights and subcellular localization suggest protective roles in inflammatory and oxidative stress conditions.
Journal, issue, pagesTo Be Published
Publish dateMar 31, 2022 (structure data deposition date)
AuthorsShafqat, N. / Dakin, S.G. / Estrada, F.M. / Niesen, F.H. / Wells, G. / Yapp, C. / Troumpra, M.K. / Brotherton, D. / Porte, S. / Mesa, J. ...Shafqat, N. / Dakin, S.G. / Estrada, F.M. / Niesen, F.H. / Wells, G. / Yapp, C. / Troumpra, M.K. / Brotherton, D. / Porte, S. / Mesa, J. / Yakovtseva, E. / Farres, J. / Pares, X. / Liu, T. / Altman, R. / Carr, A. / Koekemoer, L. / Niesen, F. / Yue, W.W. / Opperman, U.
External linksSearch PubMed
MethodsX-ray diffraction
Resolution1.79 Å
Structure data

PDB-7zej:
Crystal structure of the human MGC45594 gene product in complex with celecoxib.
Method: X-RAY DIFFRACTION / Resolution: 1.79 Å

Chemicals

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-CEL:
4-[5-(4-METHYLPHENYL)-3-(TRIFLUOROMETHYL)-1H-PYRAZOL-1-YL]BENZENESULFONAMIDE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsOXIDOREDUCTASE / alkenal reductases / prostaglandin reductases / phase 1 xenobiotic metabolism / reactive oxygen species / lipid peroxidation / polyunsaturated fatty acid / inflammation / lipid mediator metabolism / Structural Genomics / Structural Genomics Consortium / SGC

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