1aut
From Proteopedia
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HUMAN ACTIVATED PROTEIN C
Overview
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 ... [(full description)]
About this Structure
1AUT is a [Single protein] structure of sequence from [Homo sapiens]. Active as [Protein C (activated)], with EC number [3.4.21.69]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
The 2.8 A crystal structure of Gla-domainless activated protein C., Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W, EMBO J. 1996 Dec 16;15(24):6822-31. PMID:9003757
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