1aut: Difference between revisions
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'''HUMAN ACTIVATED PROTEIN C''' | {{Structure | ||
|PDB= 1aut |SIZE=350|CAPTION= <scene name='initialview01'>1aut</scene>, resolution 2.8Å | |||
|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | |||
|LIGAND= | |||
|ACTIVITY= [http://en.wikipedia.org/wiki/Protein_C_(activated) Protein C (activated)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.69 3.4.21.69] | |||
|GENE= | |||
}} | |||
'''HUMAN ACTIVATED PROTEIN C''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1AUT is a [ | 1AUT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AUT OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9003757 9003757] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein C (activated)]] | [[Category: Protein C (activated)]] | ||
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[[Category: serine proteinase)]] | [[Category: serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:02:32 2008'' | ||
Revision as of 11:02, 20 March 2008
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| , resolution 2.8Å | |||||||
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| Sites: | |||||||
| Activity: | Protein C (activated), with EC number 3.4.21.69 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HUMAN ACTIVATED PROTEIN C
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Purpura fulminans, neonatal OMIM:[176860], Thrombophilia due to protein C deficiency OMIM:[176860]
About this StructureAbout this Structure
1AUT is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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