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: 20615420DOI: 10.1016/j.jmb.2010.06.070 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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