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6F3M

Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa complexed with adenosine, K+ and Zn2+ cations

Summary for 6F3M
Entry DOI10.2210/pdb6f3m/pdb
DescriptorAdenosylhomocysteinase, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ADENOSINE, ... (9 entities in total)
Functional Keywordsregulation of sam-dependent methylation reactions, hydrolase
Biological sourcePseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Total number of polymer chains4
Total formula weight207320.94
Authors
Czyrko, J.,Brzezinski, K. (deposition date: 2017-11-28, release date: 2018-08-08, Last modification date: 2024-01-17)
Primary citationCzyrko, 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: 30054521
DOI: 10.1038/s41598-018-29535-y
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.6 Å)
Structure validation

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