_EC 3.4.24.3 Microbial collagenase. 1 PDB entries  
EC 3.-.-.- Hydrolases. [20,909 PDB entries]
EC 3.4.-.- Acting on peptide bonds (peptide hydrolases). [6,824 PDB entries]
EC 3.4.24.- Metalloendopeptidases. [608 PDB entries]
EC 3.4.24.3 Microbial collagenase. [1 PDB entries]    
3js7

Reaction: Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1'; Pro and Ala at P2 and P2'; and hydroxyproline, Ala or Arg at P3'.
Other name(s): Clostridiopeptidase A. Clostridium histolyticum collagenase. Collagenase A. Collagenase I.
Cofactor(s): Zinc.
Comments: Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum. Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class Ii has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa). The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary. The enzymes also act as peptidyl-tripeptidases. Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa,
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There are 1 PDB entries in enzyme class E.C.3.4.24.3

  PDB code Protein
3js7
Crystal structure of clostridium histolyticum colg collagena domain 2 at 1.6 angstrom resolution
Source: Clostridium histolyticum. Organism_taxid: 1498. Gene: colg. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (87 residues) CATH domain: 2.60.40.670