Alpha-lytic protease: Difference between revisions

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<StructureSection load='3pro' size='350' side='right' caption='Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry [[3pro]])' scene=''>
<StructureSection load='3pro' size='350' side='right' caption='Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry [[3pro]])' scene=''>


'''Alpha-lytic protease''' (ALP) is a bacterial serine protease of the chymotrypsin family.  ALP is a two-domain enzyme.  One domain is a large pro region (residues 1-199) that catalyzes the folding of the protease.  The second domain is the protease domain (residues 200-397).
'''Alpha-lytic protease''' (ALP) is a bacterial serine protease of the chymotrypsin family.  ALP is a two-domain enzyme.  One domain is a large pro region (residues 1-199) that catalyzes the folding of the protease.  The second domain is the protease domain (residues 200-397).<ref>PMID:2611204</ref>
</StructureSection>
</StructureSection>


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== References ==
<references/>
[[Category: Topic Page]]
[[Category: Topic Page]]

Revision as of 11:28, 3 December 2015

Structure of alpha-lytic protease protease domain (grey, green) and pro domain (yellow, pink) complex with benzenesulfonyl fluoride (PDB entry 3pro)

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3D Structures of alpha-lytic protease

Updated on 03-December-2015

References

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky