Solution structure of the epsilon subunit of the F1-atpase from thermosynechococcus elongatus BP-1

Summary for 2RQ6

DescriptorATP synthase epsilon chain (1 entity in total)
Functional Keywordsatp synthase, f1fo atp synthase, f1-atpase, epsilon subunit, atp synthesis, cf1, hydrogen ion transport, hydrolase, ion transport, membrane, thylakoid, transport, cf(1)
Biological sourceThermosynechococcus elongatus
Cellular locationCellular thylakoid membrane; Peripheral membrane protein Q8DLG7
Total number of polymer chains1
Total molecular weight14764.8
Yagi, H.,Konno, H.,Murakami-Fuse, T.,Oroguchi, H.,Akutsu, T.,Ikeguchi, M.,Hisabori, T. (deposition date: 2009-03-03, release date: 2010-01-12, Last modification date: 2011-07-13)
Primary citation
Yagi, H.,Konno, H.,Murakami-Fuse, T.,Isu, A.,Oroguchi, T.,Akutsu, H.,Ikeguchi, M.,Hisabori, T.
Structural and functional analysis of the intrinsic inhibitor subunit epsilon of F1-ATPase from photosynthetic organisms.
Biochem.J., 425:85-94, 2010
PubMed: 19785575 (PDB entries with the same primary citation)
DOI: 10.1042/BJ20091247
MImport into Mendeley
Experimental method

Structure validation

ClashscoreRamachandran outliersSidechain outliers131.2%26.4%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures