Table 4. Residues surrounding Antimycin at the Qi site.
For each contact closer than 4 Å is given the residue type, number, and atom; the atom of antimycin, and the contact distance in each monomer. For distances greater than 3 Å, only the closest contact of each protein residue is given. Except for waters, all the residues contacting antimycin belong to cyt b (chains C and P). The “water” modeled between His201 and antimycin O3 does not account for the density as currently modeled (Figure 6).
Helix A and Waters (W) | Helix D & E | Heme bH | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
distance(Å) | distance(Å) | distance(Å) | ||||||||||
protein atom | Anti atom | C | P | protein atom | Anti atom | C | P | Heme atom | Anti atom | C | P | |
ALA17 O | C10 | 3.6 | 3.7 | HEM502 | CMA | N2 | 3.8 | 3.8 | ||||
ILE27 CD1 | O2 | 3.5 | 3.5 | MET190 CG | C23 | 4.0 | 3.7 | HEM502 | CMA | C9 | 3.8 | 3.7 |
TRP31 O | N1 | 3.4 | 3.4 | MET194 CG | O9 | 3.6 | 3.5 | HEM502 | CMA | O4 | 3.2 | 3.2 |
ASN32 OD1 | C8 | 3.9 | 3.9 | LEU197 CD1 | O4 | 3.2 | 3.1 | HEM502 | CMA | C20 | 3.3 | 3.3 |
GLY34 O | C27 | 3.9 | 4.0 | SER205 OG | C4 | 3.5 | 3.5 | HEM502 | CMA | O7 | 3.7 | 3.7 |
SER35 CA | O7 | 3.0 | 3.1 | HEM502 | CMA | C27 | 3.9 | 3.9 | ||||
GLY38 CA | C27 | 3.8 | 3.8 | PHE220 CE1 | C1 | 3.3 | 3.4 | HEM502 | CAA | C5 | 3.8 | 3.9 |
LEU41 CD2 | C25 | 3.9 | 3.7 | TYR224 CD1 | O2 | 3.3 | 3.3 | HEM502 | CAA | C6 | 3.8 | 3.9 |
ASP228 OD1** | N1 | 2.8 | 2.8 | HEM502 | CAA | C7 | 3.9 | 4.0 | ||||
W3 O ** | O1 | 2.9 | 2.8 | ASP228 OD2** | O1 | 2.6 | 2.6 | HEM502 | CBA | C1 | 3.8 | 3.8 |
W1 O ** | O2 | 2.6 | 2.6 | HEM502 | CBA | C5 | 3.7 | 3.8 | ||||
“W” O | O3 | 2.6 | 2.8 | HEM502 | CBA | C6 | 3.6 | 3.6 | ||||
W1203 O | C5 | --- | 3.7 |