3APT
properties and crystal structure of methylenetetrahydrofolate reductase from Thermus thermophilus HB8
Summary for 3APT
| Entry DOI | 10.2210/pdb3apt/pdb |
| Related | 3APY |
| Descriptor | Methylenetetrahydrofolate reductase, FLAVIN-ADENINE DINUCLEOTIDE, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | tim barrel, oxidoreductase, flavin |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 70141.95 |
| Authors | Yamada, K. (deposition date: 2010-10-20, release date: 2011-09-14, Last modification date: 2023-11-01) |
| Primary citation | Igari, S.,Ohtaki, A.,Yamanaka, Y.,Sato, Y.,Yohda, M.,Odaka, M.,Noguchi, K.,Yamada, K. Properties and Crystal Structure of Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8. Plos One, 6:e23716-e23716, 2011 Cited by PubMed Abstract: Methylenetetrahydrofolate reductase (MTHFR) is one of the enzymes involved in homocysteine metabolism. Despite considerable genetic and clinical attention, the reaction mechanism and regulation of this enzyme are not fully understood because of difficult production and poor stability. While recombinant enzymes from thermophilic organisms are often stable and easy to prepare, properties of thermostable MTHFRs have not yet been reported. PubMed: 21858212DOI: 10.1371/journal.pone.0023716 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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