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PDBe Entry: 2iwz view

HUMAN MITOCHONDRIAL BETA-KETOACYL ACP SYNTHASE COMPLEXED WITH HEXANOIC ACID
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.65 Å, R-factor: 15.6%, Free R-factor: 18.8%, Spacegroup: P 21 21 21
Released 06/02/2007, deposition: 05/07/2006, last revision: 24/02/2009
Authors Christensen, C.E.search; Kragelund, B.B.search; Von Wettstein-Knowles, P.search; Henriksen, A.search
Primary citation Structure of the Human Beta-Ketoacyl [Acp] Synthase from the Mitochondrial Type II Fatty Acid Synthase.
PROTEIN SCI.search vol:16, pag:261 (2007) [PubMed ID 17242430 ]search
Keywords MITOCHONDRIAsearch, MITOCHONDRIONsearch, LIPID SYNTHESISsearch, FATTY ACID SYNTHESISsearch, FATTY ACID BIOSYNTHESISsearch, BETA-KETOACYL ACP SYNTHASEsearch, TRANSIT PEPTIDEsearch, ACYLTRANSFERASEsearch, CLAISEN CONDENSATIONsearch, KASsearch, CERULENINsearch, TRANSFERASEsearch, HOMO SAPIENSsearch
EC 2.3.1.41 ExPASy BRENDA search (A B)
Organism Homo sapiens(human) 9606search(A B)
UniProt 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial precursor (EC 2.3.1.41) (Beta-ketoacyl-ACP synthase) Q9NWU1search (A B)
Solvent A, B
Related entries 2c9h, 2iwy, 2ix4
Polymers
Id Name Type UniProt Residues Observed
A, B 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE Protein Q9NWU1 (OXSM_HUMAN)search
438 97%
Heterogens
Id Name Ligands
A, B HEXANOIC ACID 6NA search
A, B AMMONIUM ION NH4 search
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