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PDBe Entry: 1fj8 
THE STRUCTURE OF BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I IN COMPLEX WITH CERULENIN, IMPLICATIONS FOR DRUG DESIGN
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 2.27 Å, R-factor: 23.4%, Free R-factor: 26.5%, Spacegroup: P 21 21 21
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23/08/2000, deposition: 07/08/2000, last revision: 24/02/2009
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Price, A.C.; Choi, K.; Heath, R.J.; Li, Z.; White, S.W.; Rock, C.O.
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Inhibition of beta-ketoacyl-acyl carrier protein synthases by thiolactomycin and cerulenin. Structure and mechanism.
J.BIOL.CHEM. vol:276, pag:6551-6559 (2001) [PubMed ID 11050088 ]
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CONDENSING ENZYMES, FATTY ACID ELONGATION, CERULENIN, DRUG DESIGN, TRANSFERASE
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2.3.1.41 ExPASy BRENDA (A B C D)
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Escherichia coli 562(A B C D)
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3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC 2.3.1.41) (3-oxoacyl-[acyl-carrier-protein] synthase I) (Beta-ketoacyl-ACP synthase I) (KAS I) P0A953 (A B C D)
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A, B, C, D
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1fj4, 1b3n
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| A, B, C, D |
BETA-KETOACYL-[ACYL CARRIER PROTEIN] SYNTHASE I |
Protein |
P0A953 (FABB_ECOLI)
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406 |
99% |
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| A, B, C, D |
(2S, 3R)-3-HYDROXY-4-OXO-7,10-TRANS,TRANS-DODECADIENAMIDE |
CER
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