Long Spacer or Gluzincins Family

Gluzincins are proteins with the consensus HexxH( 20)E, where the third zinc ligand, a glutamate, lies at least 20 residues C-terminal to the zincin motif (Table 2). The archetypical protein of this class, thermolysin consists of two domains, with the active site located between the N-terminal catalytic domain and the all alpha C-terminal domain (Fig. 7). With the limited data available, a comparison of topological matches of the observed structures with their cor- 

The structure of thermolysin-inhibitor complexes has shown the presence of a deep PI specificity pocket and the details of hydrogen bonding between enzyme and inhibitor [28]. Side-chain atoms of the enzyme are involved in interaction with the inhibitor amides and the inhibitor conformation is such that the subsites PI and P2 both point into the enzyme core (Rg-9). 

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