2h5d: Difference between revisions

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[[Image:2h5d.jpg|left|200px]]<br /><applet load="2h5d" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2h5d.jpg|left|200px]]
caption="2h5d, resolution 0.90&Aring;" />
 
'''0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid'''<br />
{{Structure
|PDB= 2h5d |SIZE=350|CAPTION= <scene name='initialview01'>2h5d</scene>, resolution 0.90&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12]
|GENE=
}}
 
'''0.9A resolution crystal structure of alpha-lytic protease complexed with a transition state analogue, MeOSuc-Ala-Ala-Pro-Val boronic acid'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2H5D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5D OCA].  
2H5D is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2H5D OCA].  


==Reference==
==Reference==
Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16834383 16834383]
Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis., Fuhrmann CN, Daugherty MD, Agard DA, J Am Chem Soc. 2006 Jul 19;128(28):9086-102. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16834383 16834383]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Alpha-lytic endopeptidase]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
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[[Category: ultra-high resolution]]
[[Category: ultra-high resolution]]


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