6F3N
Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa cocrystallized with SAH in the presence of K+ and Zn2+ cations
Summary for 6F3N
Entry DOI | 10.2210/pdb6f3n/pdb |
Descriptor | Adenosylhomocysteinase, POTASSIUM ION, ZINC ION, ... (8 entities in total) |
Functional Keywords | regulation of sam-dependent methylation reactions, hydrolase |
Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) |
Total number of polymer chains | 4 |
Total formula weight | 211552.79 |
Authors | Czyrko, J.,Brzezinski, K. (deposition date: 2017-11-28, release date: 2018-08-08, Last modification date: 2024-05-08) |
Primary citation | Czyrko, J.,Sliwiak, J.,Imiolczyk, B.,Gdaniec, Z.,Jaskolski, M.,Brzezinski, K. Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa. Sci Rep, 8:11334-11334, 2018 Cited by PubMed: 30054521DOI: 10.1038/s41598-018-29535-y PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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