GCP II | Streptomyces | Vibrio | Comments |
---|---|---|---|
Arg-463 | Asp-173 | Ile-193 | |
Lys-499 | Glu-198 | Cys-223 | |
Lys-500 | |||
Ser-501 | Asp-200 | Tyr-225 | Hydroxamate |
Asn-519 | Arg-202 | Cys-227 | H2PO4 − |
Arg-536 | Gly-217 | Met-242 | |
Thr-538 | Phe-219 | Phe-244 | |
Lys-545 | Gly-223 | Phe-248 |
Amino acids proposed to make up part of the specificity pocket in GCP II are based on the corresponding residues observed in the crystal structure for the Vibrio aminopeptidase (Chevrier et al., 1994). Assignment of residues in Streptomyces is based on the superimposition and amino acid sequence alignment to the Vibrio aminopeptidase (Greenblatt et al., 1997). The carbonyl oxygen of Arg-202 in Streptomyces hydrogen bonds with the zinc bound H2PO4 −. In contrast to putative zinc ligands and adjacent residues that are indicated in Table 1, putative substrate ligands are not conserved. See legend for Table 1 for description of Comments.