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4BKR

Enoyl-ACP reductase from Yersinia pestis (wildtype, removed Histag) with cofactor NADH

Summary for 4BKR
Entry DOI10.2210/pdb4bkr/pdb
Related4BKO 4BKQ 4BKU
DescriptorPUTATIVE REDUCTASE YPZ3_3519, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, GLYCEROL, ... (6 entities in total)
Functional Keywordsoxidoreductase, fatty acid biosynthesis, enoyl-acp reductase
Biological sourceYERSINIA PESTIS
Total number of polymer chains1
Total formula weight45154.59
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 citationNeckles, 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: 27136302
DOI: 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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