1aix: Difference between revisions

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[[Image:1aix.gif|left|200px]]<br /><applet load="1aix" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1aix.gif|left|200px]]
caption="1aix, resolution 2.1&Aring;" />
 
'''HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL'''<br />
{{Structure
|PDB= 1aix |SIZE=350|CAPTION= <scene name='initialview01'>1aix</scene>, resolution 2.1&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=T19:PHENYLMETHYLENECARBOXY-(METHYLENEAMINO-FORMYL-DIPHENYLMETHYL)METHY-PRO-BOROVAL'>T19</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5]
|GENE=
}}
 
'''HUMAN ALPHA-THROMBIN TERNARY COMPLEX WITH EXOSITE INHIBITOR HIRUGEN AND ACTIVE SITE INHIBITOR PHCH2OCO-D-DPA-PRO-BOROVAL'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1AIX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=T19:'>T19</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Thrombin Thrombin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.5 3.4.21.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIX OCA].  
1AIX is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIX OCA].  


==Reference==
==Reference==
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships., Bode W, Turk D, Karshikov A, Protein Sci. 1992 Apr;1(4):426-71. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1304349 1304349]
The refined 1.9-A X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships., Bode W, Turk D, Karshikov A, Protein Sci. 1992 Apr;1(4):426-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1304349 1304349]
[[Category: Hirudo medicinalis]]
[[Category: Hirudo medicinalis]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: hydrolase (serine proteinase)]]
[[Category: hydrolase (serine proteinase)]]


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