_EC 3.4.21.50 Lysyl endopeptidase. 5 PDB entries  
EC 3.-.-.- Hydrolases. [21,057 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,846 PDB entries]
EC 3.4.21.- Serine endopeptidases. [2,535 PDB entries]
EC 3.4.21.50 Lysyl endopeptidase. [5 PDB entries]    
1arb

Reaction: Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
Other name(s): Achromobacter proteinase I. Lysyl bond specific proteinase.
Comments: Isolated from Achromobacter lyticus. Enzymes with similar specificity are produced by Lysobacter enzymogenes (endoproteinase Lys-C) and Pseudomonas aeruginosa (Ps-1). Belongs to peptidase family S1.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 5 PDB entries in enzyme class E.C.3.4.21.50

  PDB code Protein
1arb
The primary structure and structural characteristics of achromobacter lyticus protease i, a lysine-specific serine protease
Source: Achromobacter lyticus. Organism_taxid: 224
Chain: A (263 residues) CATH domains: 2.40.10.10 2.40.10.10
1arc
The primary structure and structural characteristics of achr lyticus protease i, a lysine-specific serine protease
Source: Achromobacter lyticus. Organism_taxid: 224
Chain: A (263 residues) CATH domains: 2.40.10.10 2.40.10.10
4gpg
X/n joint refinement of achromobacter lyticus protease i fre pd8.0
Source: Achromobacter lyticus. Organism_taxid: 224. Strain: m497-1. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (263 residues) CATH domains: 2.40.10.10 2.40.10.10
4nsv
Lysobacter enzymogenes lysc endoproteinase k30r mutant coval inhibited by tlck
Source: Lysobacter enzymogenes. Organism_taxid: 69. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (264 residues) CATH domains: 2.40.10.10 2.40.10.10
4nsy
Wild-type lysobacter enzymogenes lysc endoproteinase covalen inhibited by tlck
Source: Lysobacter enzymogenes. Organism_taxid: 69. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (264 residues) CATH domains: 2.40.10.10 2.40.10.10