1A4I
HUMAN TETRAHYDROFOLATE DEHYDROGENASE / CYCLOHYDROLASE
1A4I の概要
| エントリーDOI | 10.2210/pdb1a4i/pdb |
| 分子名称 | METHYLENETETRAHYDROFOLATE DEHYDROGENASE / METHENYLTETRAHYDROFOLATE CYCLOHYDROLASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total) |
| 機能のキーワード | thf, bifunctional, dehydrogenase, cyclohydrolase, folate, oxidoreductase |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Cytoplasm: P11586 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 66791.93 |
| 構造登録者 | |
| 主引用文献 | Allaire, M.,Li, Y.,MacKenzie, R.E.,Cygler, M. The 3-D structure of a folate-dependent dehydrogenase/cyclohydrolase bifunctional enzyme at 1.5 A resolution. Structure, 6:173-182, 1998 Cited by PubMed Abstract: The interconversion of two major folate one-carbon donors occurs through the sequential activities of NAD(P)-dependent methylene[H4]folate dehydrogenase (D) and methenyl[H4]folate cyclohydrolase (C). These activities often coexist as part of a multifunctional enzyme and there are several lines of evidence suggesting that their substrates bind at overlapping sites. Little is known, however, about the nature of this site or the identity of the active-site residues for this enzyme family. PubMed: 9519408DOI: 10.1016/S0969-2126(98)00019-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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