Table 2.
Protein | Active sites | Corresponding position and color in Fig. 3 | Active-site references |
---|---|---|---|
T4 lysozyme | Glu-11 | Coil between helix A and β-sheet (grey) | 34 |
Asp-20 | Coil in β-hairpin (red) | ||
Thr-26 | Coil in the β-hairpin (red) | ||
Myoglobin | Val-68 | α-helix E (red) | 35 |
His-93 | α-helix G (red) | ||
Ile-107 | α-helix H (red) | ||
HIV proteinase | Asp-25 | Coil between G and C terminus (blue) | 36 |
Lactoferrin | Asp-60 | Coil (green) | 37 |
Tyr-92 | Hinge β-strand (blue) | ||
Tyr-192 | Terminus of the helix (green) | ||
His-253 | Hinge (green) | ||
Barnase | Glu-73 | In β-strand E (red) | 38 |
His-102 | Coil at the C terminus (blue) |
The catalytic/binding residues at the binding sites. In barnase, HIV proteinase, and T4 lysozyme, these are the catalytic residues. In lactoferrin and myoglobin, these residues are involved in binding iron or heme. The corresponding color-coded assignments in Fig. 3 are noted.