2QSK
Atomic-resolution crystal structure of the Recombinant form of Scytovirin
2QSK の概要
| エントリーDOI | 10.2210/pdb2qsk/pdb |
| 関連するPDBエントリー | 2QT4 |
| 分子名称 | scytovirin, CHLORIDE ION, GLYCEROL, ... (4 entities in total) |
| 機能のキーワード | lectin, sugar binding protein |
| 由来する生物種 | Scytonema varium |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 9931.95 |
| 構造登録者 | Moulaei, T.,Botos, I.,Ziolkowska, N.E.,Dauter, Z.,Wlodawer, A. (登録日: 2007-07-31, 公開日: 2007-11-27, 最終更新日: 2024-10-30) |
| 主引用文献 | Moulaei, T.,Botos, I.,Ziolkowska, N.E.,Bokesch, H.R.,Krumpe, L.R.,McKee, T.C.,O'Keefe, B.R.,Dauter, Z.,Wlodawer, A. Atomic-resolution crystal structure of the antiviral lectin scytovirin. Protein Sci., 16:2756-2760, 2007 Cited by PubMed Abstract: The crystal structures of the natural and recombinant antiviral lectin scytovirin (SVN) were solved by single-wavelength anomalous scattering and refined with data extending to 1.3 A and 1.0 A resolution, respectively. A molecule of SVN consists of a single chain 95 amino acids long, with an almost perfect sequence repeat that creates two very similar domains (RMS deviation 0.25 A for 40 pairs of Calpha atoms). The crystal structure differs significantly from a previously published NMR structure of the same protein, with the RMS deviations calculated separately for the N- and C-terminal domains of 5.3 A and 3.7 A, respectively, and a very different relationship between the two domains. In addition, the disulfide bonding pattern of the crystal structures differs from that described in the previously published mass spectrometry and NMR studies. PubMed: 17965185DOI: 10.1110/ps.073157507 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1 Å) |
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