Structural characterization of the subunit A mutant F236A of the A-ATP synthase from Pyrococcus horikoshii

Summary for 3MFY

Related1VDZ 3I72 3I4L 3I73 3IKJ
DescriptorV-type ATP synthase alpha chain, (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
Functional Keywordsa-type atp synthase, p loop, phenylalanine mutant, hydrolase
Biological sourcePyrococcus horikoshii
Total number of polymer chains1
Total molecular weight66472.78
Balakrishna, A.M.,Kumar, A.,Manimekali, M.S.S.,Jeyakanthan, J.,Gruber, G. (deposition date: 2010-04-05, release date: 2010-07-07, Last modification date: 2017-08-23)
Primary citation
Kumar, A.,Manimekalai, M.S.,Balakrishna, A.M.,Priya, R.,Biukovic, G.,Jeyakanthan, J.,Gruber, G.
The critical roles of residues P235 and F236 of subunit A of the motor protein A-ATP synthase in P-loop formation and nucleotide binding.
J.Mol.Biol., 401:892-905, 2010
PubMed: 20615420 (PDB entries with the same primary citation)
DOI: 10.1016/j.jmb.2010.06.070
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.29823 2.4% 8.3% 12.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-11-25