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1AIN

CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION

1AIN の概要
エントリーDOI10.2210/pdb1ain/pdb
分子名称ANNEXIN I, CALCIUM ION (2 entities in total)
機能のキーワードcalcium/phospholipid binding, calcium-phospholipid binding complex
由来する生物種Homo sapiens (human)
細胞内の位置Nucleus (By similarity): P04083
タンパク質・核酸の鎖数1
化学式量合計35333.59
構造登録者
Kim, S.-H. (登録日: 1992-06-03, 公開日: 1993-07-15, 最終更新日: 2024-02-07)
主引用文献Weng, X.,Luecke, H.,Song, I.S.,Kang, D.S.,Kim, S.H.,Huber, R.
Crystal structure of human annexin I at 2.5 A resolution.
Protein Sci., 2:448-458, 1993
Cited by
PubMed Abstract: cDNA coding for N-terminally truncated human annexin I, a member of the family of Ca(2+)-dependent phospholipid binding proteins, has been cloned and expressed in Escherichia coli. The expressed protein is biologically active, and has been purified and crystallized in space group P2(1)2(1)2(1) with cell dimensions a = 139.36 A, b = 67.50 A, and c = 42.11 A. The crystal structure has been determined by molecular replacement at 3.0 A resolution using the annexin V core structure as the search model. The average backbone deviation between these two structures is 2.34 A. The structure has been refined to an R-factor of 17.7% at 2.5 A resolution. Six calcium sites have been identified in the annexin I structure. Each is located in the loop region of the helix-loop-helix motif. Two of the six calcium sites in annexin I are not occupied in the annexin V structure. The superpositions of the corresponding loop regions in the four domains show that the calcium binding loops in annexin I can be divided into two classes: type II and type III. Both classes are different from the well-known EF-hand motif (type I).
PubMed: 8453382
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.5 Å)
構造検証レポート
Validation report summary of 1ain
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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