Skip to main content
. Author manuscript; available in PMC: 2006 Jun 27.
Published in final edited form as: J Mol Biol. 2005 Aug 19;351(3):573–597. doi: 10.1016/j.jmb.2005.05.053

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