1HLE

CRYSTAL STRUCTURE OF CLEAVED EQUINE LEUCOCYTE ELASTASE INHIBITOR DETERMINED AT 1.95 ANGSTROMS RESOLUTION

1HLE の概要

• エントリーDOI: 10.2210/pdb1hle/pdb
• 分子名称: HORSE LEUKOCYTE ELASTASE INHIBITOR, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: hydrolase inhibitor(serine proteinase)
• 由来する生物種: Equus caballus (horse); 詳細
• 細胞内の位置: Cytoplasm : P05619 P05619
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42636.66

構造登録者

Baumann, U.,Bode, W.,Huber, R.,Travis, J.,Potempa, J. (登録日: 1992-04-13, 公開日: 1994-01-31, 最終更新日: 2024-11-13)

主引用文献

Baumann, U.,Bode, W.,Huber, R.,Travis, J.,Potempa, J.
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.
J.Mol.Biol., 226:1207-1218, 1992

PubMed Abstract: The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more precise description of the so-called R-state of the serpins.

PubMed: 1518052
DOI: 10.1016/0022-2836(92)91062-T

実験手法

X-RAY DIFFRACTION (1.95 Å)