1YTT
YB SUBSTITUTED SUBTILISIN FRAGMENT OF MANNOSE BINDING PROTEIN-A (SUB-MBP-A), MAD STRUCTURE AT 110K
1YTT の概要
| エントリーDOI | 10.2210/pdb1ytt/pdb |
| 分子名称 | MANNOSE-BINDING PROTEIN A, YTTERBIUM (III) ION (3 entities in total) |
| 機能のキーワード | carbohydrate, recognition domain, calcium dependent, mannose-binding protein |
| 由来する生物種 | Rattus norvegicus (Norway rat) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 26068.46 |
| 構造登録者 | Burling, F.T.,Weis, W.I.,Flaherty, K.M.,Brunger, A.T. (登録日: 1995-11-09, 公開日: 1996-06-10, 最終更新日: 2024-10-23) |
| 主引用文献 | Burling, F.T.,Weis, W.I.,Flaherty, K.M.,Brunger, A.T. Direct observation of protein solvation and discrete disorder with experimental crystallographic phases. Science, 271:72-77, 1996 Cited by PubMed Abstract: A complete and accurate set of experimental crystallographic phases to a resolution of 1.8 angstroms was obtained for a 230-residue dimeric fragment of rat mannose-binding protein A with the use of multiwavelength anomalous dispersion (MAD) phasing. An accurate image of the crystal structure could thus be obtained without resort to phases calculated from a model. Partially reduced disulfide bonds, local disorder, and differences in the mobility of chemically equivalent molecules are apparent in the experimental electron density map. A solvation layer is visible that includes well-ordered sites of hydration around polar and charged protein atoms, as well as diffuse, partially disordered solvent shells around exposed hydrophobic groups. Because the experimental phases and the resulting electron density map are free from the influence of a model, they provide a stringent test of theoretical models of macromolecular solvation, motion, and conformational heterogeneity. PubMed: 8539602主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.8 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






