3SDZ
Structural characterization of the subunit A mutant F427W of the A-ATP synthase from Pyrococcus horikoshii
Summary for 3SDZ
| Entry DOI | 10.2210/pdb3sdz/pdb |
| Related | 1VDZ 3I4L 3I72 3I73 |
| Descriptor | V-type ATP synthase alpha chain, (4S)-2-METHYL-2,4-PENTANEDIOL, ACETIC ACID, ... (5 entities in total) |
| Functional Keywords | a-type atp synthase, adenine-binding pocket, phenylalanine mutant, hydrolase |
| Biological source | Pyrococcus horikoshii More |
| Total number of polymer chains | 1 |
| Total formula weight | 67150.49 |
| Authors | Tadwal, V.S.,Manimekalai, M.S.S.,Balakrishna, A.M.,Gruber, G. (deposition date: 2011-06-09, release date: 2012-01-25, Last modification date: 2023-11-01) |
| Primary citation | Tadwal, V.S.,Manimekalai, M.S.,Gruber, G. Engineered tryptophan in the adenine-binding pocket of catalytic subunit A of A-ATP synthase demonstrates the importance of aromatic residues in adenine binding, forming a tool for steady-state and time-resolved fluorescence spectroscopy. Acta Crystallogr.,Sect.F, 67:1485-1491, 2011 Cited by PubMed: 22139149DOI: 10.1107/S1744309111039595 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.53 Å) |
Structure validation
Download full validation report
