1AUT

Human activated protein C

1AUT の概要

• エントリーDOI: 10.2210/pdb1aut/pdb
• 関連するBIRD辞書のPRD_ID: PRD_000020
• 分子名称: ACTIVATED PROTEIN C, D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide, ... (4 entities in total)
• 機能のキーワード: serine proteinase, plasma calcium binding, glycoprotein, hydrolase-hydrolase inhibitor complex, blood clotting, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41275.74

構造登録者

Mather, T.,Oganessyan, V.,Hof, P.,Bode, W.,Huber, R.,Foundling, S.,Esmon, C. (登録日: 1996-06-08, 公開日: 1997-08-20, 最終更新日: 2024-10-23)

主引用文献

Mather, T.,Oganessyan, V.,Hof, P.,Huber, R.,Foundling, S.,Esmon, C.,Bode, W.
The 2.8 A crystal structure of Gla-domainless activated protein C.
EMBO J., 15:6822-6831, 1996

PubMed Abstract: The structure of the Gla-domainless form of the human anticoagulant enzyme activated protein C has been solved at 2.8 A resolution. The light chain is composed of two domains: an epidermal growth factor (EGF)-like domain modified by a large insert containing an additional disulfide, followed by a typical EGF-like domain. The arrangement of the long axis of these domains describes an angle of approximately 80 degrees. Disulfide linked to the light chain is the catalytic domain, which is generally trypsin-like but contains a large insertion loop at the edge of the active site, a third helical segment, a prominent cationic patch analogous to the anion binding exosite I of thrombin and a trypsin-like Ca[II] binding site. The arrangement of loops around the active site partially restricts access to the cleft. The S2 and S4 subsites are much more polar than in factor Xa and thrombin, and the S2 site is unrestricted. While quite open and exposed, the active site contains a prominent groove, the surface of which is very polar with evidence for binding sites on the primed side, in addition to those typical of the trypsin class found on the non-primed side.

PubMed: 9003757

実験手法

X-RAY DIFFRACTION (2.8 Å)