1FNY
LEGUME LECTIN OF THE BARK OF ROBINIA PSEUDOACACIA.
1FNY の概要
| エントリーDOI | 10.2210/pdb1fny/pdb |
| 関連するPDBエントリー | 1FNZ |
| 分子名称 | BARK AGGLUTININ I,POLYPEPTIDE A, CALCIUM ION (3 entities in total) |
| 機能のキーワード | legume lectin, jelly roll, sugar binding protein |
| 由来する生物種 | Robinia pseudoacacia |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 25650.68 |
| 構造登録者 | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J. (登録日: 2000-08-24, 公開日: 2001-08-24, 最終更新日: 2024-03-13) |
| 主引用文献 | Rabijns, A.,Verboven, C.,Rouge, P.,Barre, A.,Van Damme, E.J.,Peumans, W.J.,De Ranter, C.J. Structure of a legume lectin from the bark of Robinia pseudoacacia and its complex with N-acetylgalactosamine. Proteins, 44:470-478, 2001 Cited by PubMed Abstract: The structure of the bark lectin RPbAI (isoform A4) from Robinia pseudoacacia has been determined by protein crystallography both in the free form and complexed with N-acetylgalactosamine. The free form is refined at 1.80 A resolution to an R-factor of 18.9% whereas the complexed structure has an R-factor of 19.7% at 2.05 A resolution. Both structures are compared to each other and to other available legume lectin structures. The polypeptide chains of the two structures exhibit the characteristic legume lectin tertiary fold. The quaternary structure resembles that of the Phaseolus vulgaris lectin, the soybean agglutinin, and the Dolichos biflorus lectin, but displays some unique features leading to the extreme stability of this lectin. PubMed: 11484224DOI: 10.1002/prot.1112 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.81 Å) |
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