Alpha-lytic protease: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Michal Harel (talk | contribs)
No edit summary
Michal Harel (talk | contribs)
No edit summary
Line 1: Line 1:
<StructureSection load='3pro' size='350' side='right' caption='Structure of alpha-lytic protease complex with peptidyl-boronic acid inhibitor and sulfate (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).

Revision as of 09:42, 29 October 2015

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

Drag the structure with the mouse to rotate

3D Structures of alpha-lytic protease

Updated on 29-October-2015

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky