Answer:
Another Asp in something like a deep pocket; a superficial amino acid binding pocket with either a slight neutral side, neither elastase nor trypsin.
Step-by-step explanation:
- Almost all trypsin as well as elastase contain catalytic triads. In trypsin, aspartate is the essential amino acid throughout the bag. The latter's pocket also becomes unique to charged particles (+) side-chain creatures.
- Elastase seems to have a pocket which really combines multiple valine residues, making it extremely difficult to reach the pocket with large bulky main chain, this therefore prefers short side chains.
The homologs with chymotrypsin include trypsin but mostly elastase. As either a central amino acid, chymotrypsin encompasses serine.