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).[1]
(PDB entry 3pro).
| |
3D Structures of alpha-lytic protease3D Structures of alpha-lytic protease
Updated on 06-December-2015
{"openlevels":0}
- ALP protease domain
- 2alp, 1p09, 1tal, 2ull, 1boq, 1ssz, 2h5c, 1ssx – LeALP – Lysobacter enzymogenes
- 1gba, 1gbe, 1gbj, 3urc, 3urd, 3ure, 1qq4 – 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 pro region
- ALP pro+protease domains
ReferencesReferences
- ↑ Bone R, Frank D, Kettner CA, Agard DA. Structural analysis of specificity: alpha-lytic protease complexes with analogues of reaction intermediates. Biochemistry. 1989 Sep 19;28(19):7600-9. PMID:2611204