3M4Y

Structural characterization of the subunit A mutant P235A of the A-ATP synthase

Summary for 3M4Y

Entry DOI	10.2210/pdb3m4y/pdb
Related	1VDZ 3I4L 3I72 3I73 3IKJ
Descriptor	V-type ATP synthase alpha chain, (4S)-2-METHYL-2,4-PENTANEDIOL, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, ... (5 entities in total)
Functional Keywords	hydrolase, atp synthesis, atp-binding, autocatalytic cleavage, hydrogen ion transport, intron homing, ion transport, nuclease, nucleotide-binding, transport
Biological source	Pyrococcus horikoshii OT3 More
Total number of polymer chains	1
Total formula weight	66364.57
Authors	Manimekalai, M.S.,Balakrishna, A.M.,Kumar, A.,Priya, R.,Biukovic, G.,Jeyakanthan, J.,Gruber, G. (deposition date: 2010-03-12, release date: 2011-01-26, Last modification date: 2023-11-01)
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 Cited by PubMed: 20615420 DOI: 10.1016/j.jmb.2010.06.070 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.38 Å)

Structure validation