5TOV
Crystal structure of the inactive form of S-adenosyl-L-homocysteine hydrolase from Thermotoga maritima in binary complex with NADH
Summary for 5TOV
Entry DOI | 10.2210/pdb5tov/pdb |
Descriptor | Adenosylhomocysteinase, 1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | regulation of sam-dependent methylation reactions, hydrolase |
Biological source | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
Total number of polymer chains | 2 |
Total formula weight | 91094.04 |
Authors | Czyrko, J.,Brzezinski, K. (deposition date: 2016-10-19, release date: 2017-07-05, Last modification date: 2024-01-17) |
Primary citation | Brzezinski, K.,Czyrko, J.,Sliwiak, J.,Nalewajko-Sieliwoniuk, E.,Jaskolski, M.,Nocek, B.,Dauter, Z. S-adenosyl-L-homocysteine hydrolase from a hyperthermophile (Thermotoga maritima) is expressed in Escherichia coli in inactive form - Biochemical and structural studies. Int. J. Biol. Macromol., 104:584-596, 2017 Cited by PubMed: 28629859DOI: 10.1016/j.ijbiomac.2017.06.065 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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