1MZS

CRYSTAL STRUCTURE OF BETA-KETOACYL-ACP SYNTHASE III WITH BOUND dichlorobenzyloxy-indole-carboxylic acid inhibitor

Summary for 1MZS

• Entry DOI: 10.2210/pdb1mzs/pdb
• Related: 1hn9 1hnd 1hnh 1hnj
• Descriptor: 3-oxoacyl-[acyl-carrier-protein] synthase III, PHOSPHATE ION, 1-(5-CARBOXYPENTYL)-5-(2,6-DICHLOROBENZYLOXY)-1H-INDOLE-2-CARBOXYLIC ACID, ... (4 entities in total)
• Functional Keywords: fabh, transferase
• Biological source: Escherichia coli
• Cellular location: Cytoplasm : P0A6R0
• Total number of polymer chains: 1
• Total formula weight: 34140.31

Authors

Daines, R.A.,Pendrak, I.,Sham, K.,Van Aller, G.S.,Konstantinidis, A.K.,Lonsdale, J.T.,Janson, C.A.,Qui, X.,Brandt, M.,Silverman, C.,Head, M.S. (deposition date: 2002-10-09, release date: 2002-11-13, Last modification date: 2017-10-11)

Primary citation

Daines, R.A.,Pendrak, I.,Sham, K.,Van Aller, G.S.,Konstantinidis, A.K.,Lonsdale, J.T.,Janson, C.A.,Qiu, X.,Brandt, M.,Khandekar, S.S.,Silverman, C.,Head, M.S.
First X-ray cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor achieved using rational design and homology modeling
J.Med.Chem., 46:5-8, 2003

PubMed Abstract: The first cocrystal structure of a bacterial FabH condensing enzyme and a small molecule inhibitor is reported. The inhibitor was obtained by rational modification of a high throughput screening lead with the aid of a S. pneumoniae FabH homology model. This homology model was used to design analogues that would have both high affinity for the enzyme and appropriate aqueous solubility to facilitate cocrystallization studies.

PubMed: 12502353
DOI: 10.1021/jm025571b

Experimental method

X-RAY DIFFRACTION (2.1 Å)