Alpha-lytic protease

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).

spinqualitylabelsall models Structure of alpha-lytic protease complex with peptidyl-boronic acid inhibitor and sulfate (PDB entry 3pro) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D Structures of alpha-lytic protease3D Structures of alpha-lytic protease

Updated on 29-October-2015

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• 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
  • 2pro, 1qrx – LeALP pro region
    
  • 1qrw, 3m7t, 3m7u – LeALP pro region (mutant)
    
• ALP pro+protease domains
  • 3pro, 4pro – LeALP (mutant)