1AUT

Human activated protein C

Summary for 1AUT

• Entry DOI: 10.2210/pdb1aut/pdb
• Related PRD ID: PRD_000020
• Descriptor: 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)
• Functional Keywords: serine proteinase, plasma calcium binding, glycoprotein, hydrolase-hydrolase inhibitor complex, blood clotting, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 41275.74

Authors

Mather, T.,Oganessyan, V.,Hof, P.,Bode, W.,Huber, R.,Foundling, S.,Esmon, C. (deposition date: 1996-06-08, release date: 1997-08-20, Last modification date: 2024-10-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.8 Å)