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 that catalyzes the folding of the protease. The second domain is the protease domain.
3D Structures of alpha-lytic protease
Updated on 29-January-2014
ALP protease domain
2alp, 1p09, 1tal, 2ull, 1boq, 1ssz, 2h5c, 1ssx – LeALP – Lysobacter enzymogenes
1gba, 1gbe, 1gbj, 3urc, 3urd, 3ure – LeALP (mutant)
1p01, 1p02, 1p03, 1p04, 1p05, 1p06, 1p10, 2lpr, 3lpr, 5lpr, 6lpr, 7lpr, 8lpr, 9lpr, 2h5d – LeALP + boronic acid inhibitor
1gbb, 1gbc, 1gbd, 1gbf, 1gbh, 1gbi, 1gbk, 1gbl, 1gbm – LeALP (mutant) + boronic acid inhibitor
1p11, 1p12 – LeALP + phosphonate esther inhibitor
3qgj – LeALP + peptide
ALP including pro region
2pro, 1qrx – LeALP pro region
1qq4, 1qrw, 3m7t, 3m7u – LeALP pro region (mutant)
3pro – LeALP (mutant) + pro region
4pro – LeALP (mutant) + pro region (mutant)
