1DLM
STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER CALCOACETICUS NATIVE DATA
1DLM の概要
エントリーDOI | 10.2210/pdb1dlm/pdb |
関連するPDBエントリー | 1DLM 1DLQ 1DLT 1DMH |
分子名称 | CATECHOL 1,2-DIOXYGENASE, FE (III) ION, [1-PENTADECANOYL-2-DECANOYL-GLYCEROL-3-YL]PHOSPHONYL CHOLINE, ... (4 entities in total) |
機能のキーワード | metalloprotein, dioxygenase, aromatic compound degradation, mixed alpha helix/ beta strand, oxidoreductase |
由来する生物種 | Acinetobacter sp. |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 70153.70 |
構造登録者 | |
主引用文献 | Vetting, M.W.,Ohlendorf, D.H. The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker. Structure Fold.Des., 8:429-440, 2000 Cited by PubMed Abstract: Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. Catechol 1,2-dioxygenases (1, 2-CTDs) have a rudimentary design structure - a homodimer with one catalytic non-heme ferric ion per monomer, that is (alphaFe(3+))(2). This is in contrast to the archetypical intradiol dioxygenase protocatechuate 3,4-dioxygenase (3,4-PCD), which forms more diverse oligomers, such as (alphabetaFe(3+))(2-12). PubMed: 10801478DOI: 10.1016/S0969-2126(00)00122-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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