1DSU

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

1DSU の概要

• エントリーDOI: 10.2210/pdb1dsu/pdb
• 分子名称: FACTOR D (2 entities in total)
• 機能のキーワード: complement activating enzyme, hydrolase, serine protease, hydrolase (serine protease)
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted: P00746
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 48877.61

構造登録者

Narayana, S.V.L.,Volanakis, J.E.,Delucas, L.J. (登録日: 1995-09-15, 公開日: 1996-08-17, 最終更新日: 2024-10-23)

主引用文献

Narayana, S.V.,Carson, M.,el-Kabbani, O.,Kilpatrick, J.M.,Moore, D.,Chen, X.,Bugg, C.E.,Volanakis, J.E.,DeLucas, L.J.
Structure of human factor D. A complement system protein at 2.0 A resolution.
J.Mol.Biol., 235:695-708, 1994

PubMed Abstract: Factor D, an essential enzyme for the activation of the alternative pathway of the complement system, belongs to the serine protease superfamily. The crystal structure of the enzyme was solved by a combination of multiple isomorphous replacement and molecular replacement methods. The present model was refined to an R-factor of 18.8% using 23,681 observed reflections between 7.5 and 2.0 A resolution, with a root-mean-square deviation from standard bond lengths of 0.016 A. The two non-crystallographically related molecules in the triclinic unit cell have distinctive active site conformations. The protein has the general structural fold of a serine protease, but there are several unique amino acid substitutions resulting in significant alterations in the critical loops responsible for catalysis and substrate specificity in serine proteases. Factor D is the first complement serine protease whose three-dimensional structure has been determined.

PubMed: 8289289
DOI: 10.1006/jmbi.1994.1021

実験手法

X-RAY DIFFRACTION (2 Å)