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PDBe Entry: 2fad view

Crystal structure of E. coli heptanoyl-ACP
Summary
Header BIOSYNTHETIC PROTEINsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.6 Å, R-factor: 20.9%, Free R-factor: 25.6%, Spacegroup: P 21 21 2
Released 26/09/2006, deposition: 07/12/2005, last revision: 24/02/2009
Authors Roujeinikova, A.search
Primary citation Structural Studies of Fatty Acyl-(Acyl Carrier Protein) Thioesters Reveal a Hydrophobic Binding Cavity that Can Expand to Fit Longer Substrates.
J.MOL.BIOL.search vol:365, pag:135-145 (2007) [PubMed ID 17059829 ]search
Keywords acyl carrier proteinsearch, acyl chain bindingsearch, fatty acid biosynthesissearch, BIOSYNTHETIC PROTEINsearch
Organism Escherichia coli 562search(A B)
UniProt Acyl carrier protein (ACP) (Cytosolic-activating factor) (CAF) (Fatty acid synthase acyl carrier protein) P0A6A8search (A B)
Solvent A, B
Related entries 1l0h, 1l0i
Polymers
Id Name Type UniProt Residues Observed
A, B Acyl carrier protein Protein P0A6A8 (ACP_ECOLI)search
77 100%
Heterogens
Id Name Ligands
A SODIUM ION NA search
A, B ZINC ION ZN search
A, B S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) HEPTANETHIOATE PM5 search
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