2D1N

Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor

2D1N の概要

• エントリーDOI: 10.2210/pdb2d1n/pdb
• 関連するPDBエントリー: 2D1O
• 分子名称: Collagenase 3, ZINC ION, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: hydorolase metalloprotease, hydrolase
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38887.93

構造登録者

Kohno, T.,Hochigai, H.,Yamashita, E.,Tsukihara, T.,Kanaoka, M. (登録日: 2005-08-29, 公開日: 2006-06-27, 最終更新日: 2023-10-25)

主引用文献

Kohno, T.,Hochigai, H.,Yamashita, E.,Tsukihara, T.,Kanaoka, M.
Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453
Biochem.Biophys.Res.Commun., 344:315-322, 2006

PubMed Abstract: Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have been solved at 2.01 and 2.37A resolutions, respectively. The results revealed that the binding modes for this inhibitor to MMP-3 and -13 were quite similar. However, subtle comparative differences were observed at the bottom of S1' pockets, which were occupied with the guanidinomethyl moiety of the inhibitor. A remarkable feature of the inhibitor was the deep penetration of its long aliphatic chain into the S1' pocket and exposure of the guanidinomethyl moiety to the solvent.

PubMed: 16603129
DOI: 10.1016/j.bbrc.2006.03.098

実験手法

X-RAY DIFFRACTION (2.37 Å)