Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Discovery and optimization of antibacterial AccC inhibitors.
Journal, issue, pages	Bioorg. Med. Chem. Lett., Vol. 19, Page 6507-6514, Year 2009
Publish date	Sep 23, 2009 (structure data deposition date)
Authors	Cheng, C.C. / Shipps, G.W. / Yang, Z. / Sun, B. / Kawahata, N. / Soucy, K.A. / Soriano, A. / Orth, P. / Xiao, L. / Mann, P. / Black, T.
External links	Bioorg. Med. Chem. Lett. / PubMed:19875284
Methods	X-ray diffraction
Resolution	2.13 - 2.31 Å
Structure data	PDB-3jzf: Crystal structure of biotin carboxylase from E. Coli in complex with benzimidazoles series Method: X-RAY DIFFRACTION / Resolution: 2.13 Å PDB-3jzi: Crystal structure of biotin carboxylase from E. Coli in complex with benzimidazole series Method: X-RAY DIFFRACTION / Resolution: 2.31 Å
Chemicals	ChemComp-CO3: CARBONATE ION ChemComp-JZK: 2-[(2-chlorobenzyl)amino]-1-(cyclohexylmethyl)-1H-benzimidazole-5-carboxamide ChemComp-HOH: WATER ChemComp-JZL: 7-amino-2-[(2-chlorobenzyl)amino]-1-{[(1S,2S)-2-hydroxycycloheptyl]methyl}-1H-benzimidazole-5-carboxamide
Source	escherichia coli (E. coli)
Keywords	LIGASE / Biotin carboxylase / AccC / Acetyl coenzyme-A carboxylase / ACCase / ATP-binding / Biotin / Fatty acid biosynthesis / Lipid synthesis / Nucleotide-binding / Biotin carboxylase; AccC; Acetyl coenzyme-A carboxylase; ACCase;