1EBL

THE 1.8 A CRYSTAL STRUCTURE AND ACTIVE SITE ARCHITECTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE III (FABH) FROM ESCHERICHIA COLI

Summary for 1EBL

Related1D9B
DescriptorBETA-KETOACYL-ACP SYNTHASE III, COENZYME A (3 entities in total)
Functional Keywordsacyltransferase, condensing enzyme, fatty acid synthesis, lipid metabolism, alpha-beta protein, five-layered fold, coenzyme a binding protein, helix dipole, malonyl coa decarboxylating enzyme, transferase
Biological sourceEscherichia coli
Cellular locationCytoplasm  P0A6R0
Total number of polymer chains2
Total molecular weight69381.33
Authors
Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O. (deposition date: 2000-01-24, release date: 2000-02-11, Last modification date: 2018-01-31)
Primary citation
Davies, C.,Heath, R.J.,White, S.W.,Rock, C.O.
The 1.8 A crystal structure and active-site architecture of beta-ketoacyl-acyl carrier protein synthase III (FabH) from escherichia coli.
Structure Fold.Des., 8:185-195, 2000
PubMed: 10673437 (PDB entries with the same primary citation)
DOI: 10.1016/S0969-2126(00)00094-0
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers120.2%4.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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