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EBI PDBe PDBeView

PDBe Entry: 2bz4 view

STRUCTURE OF E. COLI KAS I H298Q MUTANT
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.86 Å, R-factor: 20.4%, Free R-factor: 23.4%, Spacegroup: P 21 21 21
Released 01/02/2006, deposition: 10/08/2005, last revision: 24/02/2009
Authors Olsen, J.G.search; Von Wettstein-Knowles, P.search; Henriksen, A.search
Primary citation Fatty Acid Synthesis. Role of Active Site Histidines and Lysine in Cys-His-His-Type Beta-Ketoacyl-Acyl Carrier Protein Synthases.
FEBS J.search vol:273, pag:695 (2006) [PubMed ID 16441657 ]search
Keywords TRANSFERASEsearch, ACYLTRANSFERASEsearch, CLAISEN CONDENSATIONsearch, FATTY ACID BIOSYNTHESISsearch, FATTY ACID SYNTHASEsearch, THIOLASE FOLDsearch
EC 2.3.1.41 ExPASy BRENDA search (A B C D)
Organism Escherichia coli 562search(A B C D)
UniProt 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) P0A953search (A B C D)
Solvent A, B, C, D
Related entries 1dd8, 1ek4, 1f91, 1fj4, 1fj8, 1g5x, 1h4f, 2buh, 2bui, 2byw, 2byx, 2byy, 2byz, 2bz3
Polymers
Id Name Type UniProt Residues Observed
A, B, C, D 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I Protein P0A953 (FABB_ECOLI)search
 418 97%
Heterogens
Id Name Ligands
A, B, C, D AMMONIUM ION NH4 search
C, D SULFATE ION SO4 search
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