1aut: Difference between revisions
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|PDB= 1aut |SIZE=350|CAPTION= <scene name='initialview01'>1aut</scene>, resolution 2.8Å | |PDB= 1aut |SIZE=350|CAPTION= <scene name='initialview01'>1aut</scene>, resolution 2.8Å | ||
|SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | |SITE= <scene name='pdbsite=CAT:Catalytic+Site'>CAT</scene> | ||
|LIGAND= | |LIGAND= <scene name='pdbligand=BHD:BETA-HYDROXYASPARTIC+ACID'>BHD</scene>, <scene name='pdbligand=DPN:D-PHENYLALANINE'>DPN</scene>, <scene name='pdbligand=MAI:DEOXO-METHYLARGININE'>MAI</scene> | ||
|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] | |ACTIVITY= <span class='plainlinks'>[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] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aut OCA], [http://www.ebi.ac.uk/pdbsum/1aut PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aut RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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 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 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: serine proteinase)]] | [[Category: serine proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:47:52 2008'' | ||
