1EDO
THE X-RAY STRUCTURE OF BETA-KETO ACYL CARRIER PROTEIN REDUCTASE FROM BRASSICA NAPUS COMPLEXED WITH NADP+
Summary for 1EDO
| Entry DOI | 10.2210/pdb1edo/pdb |
| Descriptor | BETA-KETO ACYL CARRIER PROTEIN REDUCTASE, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| Functional Keywords | nucleotide fold, rossmann fold, oxidoreductase |
| Biological source | Brassica napus (rape) |
| Cellular location | Plastid, chloroplast (By similarity): Q93X62 |
| Total number of polymer chains | 1 |
| Total formula weight | 26102.82 |
| Authors | Fisher, M.,Kroon, J.T.,Martindale, W.,Stuitje, A.R.,Slabas, A.R.,Rafferty, J.B. (deposition date: 2000-01-28, release date: 2001-01-31, Last modification date: 2024-02-07) |
| Primary citation | Fisher, M.,Kroon, J.T.,Martindale, W.,Stuitje, A.R.,Slabas, A.R.,Rafferty, J.B. The X-ray structure of Brassica napus beta-keto acyl carrier protein reductase and its implications for substrate binding and catalysis. Structure Fold.Des., 8:339-347, 2000 Cited by PubMed Abstract: beta-Keto acyl carrier protein reductase (BKR) catalyzes the pyridine-nucleotide-dependent reduction of a 3-oxoacyl form of acyl carrier protein (ACP), the first reductive step in de novo fatty acid biosynthesis and a reaction often performed in polyketide biosynthesis. The Brassica napus BKR enzyme is NADPH-dependent and forms part of a dissociable type II fatty acid synthetase (FAS). Significant sequence similarity is observed with enoyl acyl carrier protein reductase (ENR), the other reductase of FAS, and the short-chain alcohol dehydrogenase (SDR) family. PubMed: 10801480DOI: 10.1016/S0969-2126(00)00115-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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