4ylt

Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestisCrystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis

Structural highlights 4ylt is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Activity: [acyl-carrier-protein_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number 2.3.1.180 Resources: FirstGlance, OCA, RCSB, PDBsum Function [FABH_YERPE] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.

spinqualitylabelsall models 4ylt, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image