3S8M

The Crystal Structure of FabV

Summary for 3S8M

Entry DOI	10.2210/pdb3s8m/pdb
Descriptor	Enoyl-ACP Reductase (2 entities in total)
Functional Keywords	rossmann fold, oxidoreductase, nadh binding, fatty acid synthesis, enoyl-acp
Biological source	Xanthomonas oryzae pv. oryzae
Total number of polymer chains	1
Total formula weight	46247.07
Authors	Li, H.,Zhang, X.L.,Bi, L.J.,He, J.,Jiang, T. (deposition date: 2011-05-29, release date: 2011-11-16, Last modification date: 2024-10-16)
Primary citation	Li, H.,Zhang, X.,Bi, L.,He, J.,Jiang, T. Determination of the Crystal Structure and Active Residues of FabV, the Enoyl-ACP Reductase from Xanthomonas oryzae. Plos One, 6:e26743-e26743, 2011 Cited by PubMed Abstract: Enoyl-ACP reductase (ENR) catalyses the last reduction reaction in the fatty acid elongation cycle in bacteria and is a good antimicrobial target candidate. FabV is the most recently discovered class of ENR, but we lack information about the atomic structure and the key residues involved in reductase activity except for the known conserved tyrosine and lysine residues in the Y-X(8)-K active site motif. PubMed: 22039545 DOI: 10.1371/journal.pone.0026743 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.6 Å)

Structure validation