1nb5: Difference between revisions

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[[Image:1nb5.gif|left|200px]]<br /><applet load="1nb5" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1nb5.gif|left|200px]]
caption="1nb5, resolution 2.4&Aring;" />
 
'''Crystal structure of stefin A in complex with cathepsin H'''<br />
{{Structure
|PDB= 1nb5 |SIZE=350|CAPTION= <scene name='initialview01'>1nb5</scene>, resolution 2.4&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Cathepsin_H Cathepsin H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.16 3.4.22.16]
|GENE= CSTA OR STF1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
}}
 
'''Crystal structure of stefin A in complex with cathepsin H'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1NB5 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Active as [http://en.wikipedia.org/wiki/Cathepsin_H Cathepsin H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.16 3.4.22.16] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NB5 OCA].  
1NB5 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NB5 OCA].  


==Reference==
==Reference==
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases., Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D, J Mol Biol. 2003 Feb 21;326(3):875-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12581647 12581647]
Crystal structure of Stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo- and exopeptidases., Jenko S, Dolenc I, Guncar G, Dobersek A, Podobnik M, Turk D, J Mol Biol. 2003 Feb 21;326(3):875-85. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12581647 12581647]
[[Category: Cathepsin H]]
[[Category: Cathepsin H]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: enzyme-inhibitor complex]]
[[Category: enzyme-inhibitor complex]]


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