4BKR
Enoyl-ACP reductase from Yersinia pestis (wildtype, removed Histag) with cofactor NADH
Summary for 4BKR
Entry DOI | 10.2210/pdb4bkr/pdb |
Related | 4BKO 4BKQ 4BKU |
Descriptor | PUTATIVE REDUCTASE YPZ3_3519, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, GLYCEROL, ... (6 entities in total) |
Functional Keywords | oxidoreductase, fatty acid biosynthesis, enoyl-acp reductase |
Biological source | YERSINIA PESTIS |
Total number of polymer chains | 1 |
Total formula weight | 45154.59 |
Authors | Hirschbeck, M.W.,Neckles, C.,Tonge, P.J.,Kisker, C. (deposition date: 2013-04-29, release date: 2014-05-14, Last modification date: 2023-12-20) |
Primary citation | Neckles, C.,Pschibul, A.,Lai, C.,Hirschbeck, M.,Kuper, J.,Davoodi, S.,Zou, J.,Liu, N.,Pan, P.,Shah, S.,Daryaee, F.,Bommineni, G.R.,Lai, C.,Simmerling, C.,Kisker, C.,Tonge, P.J. Selectivity of Pyridone- and Diphenyl Ether-Based Inhibitors for the Yersinia Pestis Fabv Enoyl-Acp Reductase. Biochemistry, 55:2992-, 2016 Cited by PubMed: 27136302DOI: 10.1021/ACS.BIOCHEM.5B01301 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.798 Å) |
Structure validation
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