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3f6u
From Proteopedia
| 3f6u, resolution 2.80Å () | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||||
| Ligands: | , , | ||||||||
| Activity: | Protein C (activated), with EC number 3.4.21.69 | ||||||||
| Related: | 1aut | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Crystal structure of human Activated Protein C (APC) complexed with PPACK
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
3f6u is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- 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. 1996 Dec 16;15(24):6822-31. PMID:9003757
- Schmidt AE, Padmanabhan K, Underwood MC, Bode W, Mather T, Bajaj SP. Thermodynamic linkage between the S1 site, the Na+ site, and the Ca2+ site in the protease domain of human activated protein C (APC). Sodium ion in the APC crystal structure is coordinated to four carbonyl groups from two separate loops. J Biol Chem. 2002 Aug 9;277(32):28987-95. Epub 2002 May 23. PMID:12029084 doi:10.1074/jbc.M201892200
