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-Structure paper
Title | 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. |
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Journal, issue, pages | Acta Crystallogr. ,Sect. F, Vol. 67, Page 1485-1491, Year 2011 |
Publish date | Jun 9, 2011 (structure data deposition date) |
![]() | Tadwal, V.S. / Manimekalai, M.S. / Gruber, G. |
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Methods | X-ray diffraction |
Resolution | 2.53 - 2.62 Å |
Structure data | ![]() PDB-3sdz: ![]() PDB-3se0: |
Chemicals | ![]() ChemComp-MPD: ![]() ChemComp-ACY: ![]() ChemComp-TRS: ![]() ChemComp-HOH: ![]() ChemComp-SO4: |
Source |
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![]() | HYDROLASE / A-Type ATP synthase / Adenine-binding pocket / Phenylalanine mutant |