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 with sequence from Yersinia pestis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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. See Also Acyl carrier protein synthase 3D structures

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