Table 4.
Comparison of binding interactions for (10) in crystal and docked structures
| Distancea,b | EcMetAP1 Actual | RpMetAP1 Docked |
|---|---|---|
| Mn(II) Chelation | 2.2, 2.3 | 1.7, 2.1 |
| Mn(II) Coordination | 2.0 | 1.8 |
| π - π Stacking (Tyr62) | 4.0 | 3.1 |
| Hydrophobic (His63) | 3.5 | 6.9c |
| Hydrophobic (Tyr65) | 3.6 | 3.5 |
| Hydrophobic (His79) | 3.6 | 3.9 |
| Hydrophobic (Phe177) | 4.0 | 3.3 |
| Hydrophobic (His178) | 3.3 | 3.6 |
| Hydrophobic (Trp221) | 3.4 | 3.1 |
| Angle | ||
| Mn(II) – OL – Mn(II) Angle | 107° | 155° |
| (10) Dihedral | 41° | 18° |
a
Distances correspond to closest observed interaction and are reported in Å
b
Residue numbering corresponds to EcMetAP1 (PDB: 1XNZ)12
c
This is a non-conserved residue and exists as Lys in RpMetAP