Crystal structure of the f1-atpase from the thermoalkaliphilic bacterium bacillus sp. ta2.a1

Summary for 2QE7

Related1JNV 1SKY
DescriptorATP synthase subunit alpha, ATP synthase subunit beta, ATP synthase subunit gamma, ... (4 entities in total)
Functional Keywordsblockage of atp hydrolysis, f1-atpase, atp synthase, single particle analysis, thermoalkaliphilic, hydrolase
Biological sourceBacillus sp.
Cellular locationCell membrane; Peripheral membrane protein (By similarity) Q71CG5 Q71CG3 Q71CG4 Q71CG2
Total number of polymer chains8
Total molecular weight362763.77
Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P. (deposition date: 2007-06-25, release date: 2007-08-21, Last modification date: 2013-05-08)
Primary citation
Stocker, A.,Keis, S.,Vonck, J.,Cook, G.M.,Dimroth, P.
The Structural Basis for Unidirectional Rotation of Thermoalkaliphilic F(1)-ATPase.
Structure, 15:904-914, 2007
PubMed: 17697996 (PDB entries with the same primary citation)
DOI: 10.1016/j.str.2007.06.009
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.302362.7%10.2%7.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload