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PDBe Entry: 2alm view

Crystal structure analysis of a mutant beta-ketoacyl-[acyl carrier protein] synthase II from Streptococcus pneumoniae
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.6 Å, R-factor: 23.6%, Free R-factor: 25.7%, Spacegroup: P 21 21 2
Released 30/08/2005, deposition: 07/08/2005, last revision: 09/12/2008
Authors Zhang, Y.M.search; Hurlbert, J.search; White, S.W.search; Rock, C.O.search
Primary citation Roles of the active site water, histidine 303, and phenylalanine 396 in the catalytic mechanism of the elongation condensing enzyme of Streptococcus pneumoniae.
J.BIOL.CHEM.search vol:281, pag:17390-17399 (2006) [PubMed ID 16618705 ]search
Keywords Beta-ketoacyl-ACP synthase IIsearch, Thiolasesearch, TRANSFERASEsearch
EC 2.3.1.41 ExPASy BRENDA search (A)
Organism Streptococcus pneumoniae 1313search(A)
UniProt Beta-ketoacyl-ACP synthase II (3-oxoacyl-(Acyl-carrier-protein) synthase II) (EC 2.3.1.41) Q9FBC2search (A)
Solvent A
Related entries 1ox0
Polymers
Id Name Type UniProt Residues Observed
A 3-oxoacyl-(acyl-carrier-protein) synthase II Protein Q9FBC2 (Q9FBC2_STRPN)search
431 95%
Heterogens
Id Name Ligands
A MAGNESIUM ION MG search
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