Iron in PDB 1sqb: Crystal Structure Analysis of Bovine BC1 with Azoxystrobin

All present enzymatic activity of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin:
1.10.2.2;

The structure of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin, PDB code: 1sqb was solved by L.Esser, B.Quinn, Y.F.Li, M.Zhang, M.Elberry, L.Yu, C.A.Yu, D.Xia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.69
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	153.554, 153.554, 596.393, 90.00, 90.00, 90.00
R / Rfree (%)	24.1 / 28.8

The binding sites of Iron atom in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin (pdb code 1sqb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin, PDB code: 1sqb:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe381 b:48.8 occ:1.00 FE C:HEM381 0.0 48.8 1.0 NB C:HEM381 2.0 49.9 1.0 NC C:HEM381 2.0 48.7 1.0 ND C:HEM381 2.0 47.8 1.0 NA C:HEM381 2.0 46.6 1.0 NE2 C:HIS196 2.3 2.8 1.0 NE2 C:HIS97 2.3 8.6 1.0 C4A C:HEM381 3.0 47.5 1.0 C1A C:HEM381 3.0 47.0 1.0 C1C C:HEM381 3.0 50.0 1.0 C4B C:HEM381 3.0 50.1 1.0 C4C C:HEM381 3.0 49.0 1.0 C1B C:HEM381 3.0 50.6 1.0 C4D C:HEM381 3.0 47.0 1.0 C1D C:HEM381 3.0 48.7 1.0 CD2 C:HIS196 3.2 5.8 1.0 CD2 C:HIS97 3.2 9.1 1.0 CE1 C:HIS196 3.2 3.0 1.0 CE1 C:HIS97 3.3 8.5 1.0 CHA C:HEM381 3.4 46.4 1.0 CHB C:HEM381 3.4 50.3 1.0 CHC C:HEM381 3.4 50.7 1.0 CHD C:HEM381 3.5 48.6 1.0 C2A C:HEM381 4.2 47.5 1.0 C3A C:HEM381 4.2 47.2 1.0 C3D C:HEM381 4.2 47.9 1.0 C2D C:HEM381 4.2 49.0 1.0 C2C C:HEM381 4.2 50.5 1.0 C2B C:HEM381 4.2 51.1 1.0 C3B C:HEM381 4.3 51.1 1.0 C3C C:HEM381 4.3 49.5 1.0 ND1 C:HIS196 4.3 8.4 1.0 CG C:HIS196 4.3 8.1 1.0 CG C:HIS97 4.4 10.3 1.0 ND1 C:HIS97 4.4 10.9 1.0

Iron binding site 2 out of 5 in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe382 b:77.3 occ:1.00 FE C:HEM382 0.0 77.3 1.0 NC C:HEM382 2.0 81.0 1.0 ND C:HEM382 2.0 79.5 1.0 NA C:HEM382 2.0 81.0 1.0 NB C:HEM382 2.0 80.4 1.0 NE2 C:HIS83 2.1 2.4 1.0 NE2 C:HIS182 2.2 2.4 1.0 C1A C:HEM382 3.0 81.6 1.0 C4A C:HEM382 3.0 82.4 1.0 CE1 C:HIS83 3.0 2.6 1.0 C1C C:HEM382 3.0 81.6 1.0 C4C C:HEM382 3.1 80.7 1.0 C4D C:HEM382 3.1 79.2 1.0 C4B C:HEM382 3.1 79.9 1.0 C1B C:HEM382 3.1 80.4 1.0 C1D C:HEM382 3.1 78.5 1.0 CE1 C:HIS182 3.2 2.4 1.0 CD2 C:HIS83 3.2 2.4 1.0 CD2 C:HIS182 3.2 2.4 1.0 CHA C:HEM382 3.5 80.9 1.0 CHC C:HEM382 3.5 81.4 1.0 CHB C:HEM382 3.5 81.8 1.0 CHD C:HEM382 3.5 80.2 1.0 ND1 C:HIS83 4.2 4.8 1.0 C2A C:HEM382 4.2 82.7 1.0 C3A C:HEM382 4.2 83.1 1.0 C3D C:HEM382 4.3 76.5 1.0 ND1 C:HIS182 4.3 3.1 1.0 CG C:HIS83 4.3 4.7 1.0 C2D C:HEM382 4.3 77.2 1.0 C2B C:HEM382 4.3 79.3 1.0 C2C C:HEM382 4.3 81.1 1.0 C3C C:HEM382 4.3 81.0 1.0 C3B C:HEM382 4.3 79.1 1.0 CG C:HIS182 4.3 3.9 1.0 OE1 C:GLN44 4.8 7.0 1.0 CA C:GLY48 5.0 12.5 1.0

Iron binding site 3 out of 5 in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe242 b:70.1 occ:1.00 FE D:HEM242 0.0 70.1 1.0 NB D:HEM242 2.0 68.0 1.0 NC D:HEM242 2.0 71.3 1.0 ND D:HEM242 2.0 68.8 1.0 NA D:HEM242 2.0 69.9 1.0 NE2 D:HIS41 2.3 7.3 1.0 SD D:MET160 2.6 14.4 1.0 C1A D:HEM242 3.0 69.9 1.0 C4A D:HEM242 3.0 69.5 1.0 C1B D:HEM242 3.0 68.8 1.0 C4B D:HEM242 3.0 68.2 1.0 C4D D:HEM242 3.0 68.9 1.0 C1C D:HEM242 3.0 71.9 1.0 C4C D:HEM242 3.0 72.0 1.0 C1D D:HEM242 3.0 70.7 1.0 CD2 D:HIS41 3.1 7.5 1.0 CE1 D:HIS41 3.3 6.8 1.0 CHA D:HEM242 3.4 69.4 1.0 CHC D:HEM242 3.5 70.0 1.0 CHB D:HEM242 3.5 69.1 1.0 CHD D:HEM242 3.5 71.6 1.0 CG D:MET160 3.7 12.5 1.0 CE D:MET160 4.0 13.1 1.0 CB D:MET160 4.2 12.1 1.0 C2A D:HEM242 4.2 70.4 1.0 C3D D:HEM242 4.2 70.0 1.0 C3A D:HEM242 4.2 70.0 1.0 C2B D:HEM242 4.2 68.6 1.0 C3B D:HEM242 4.2 69.8 1.0 C2D D:HEM242 4.3 70.4 1.0 C2C D:HEM242 4.3 72.2 1.0 CG D:HIS41 4.3 9.1 1.0 C3C D:HEM242 4.3 73.4 1.0 ND1 D:HIS41 4.3 8.1 1.0

Iron binding site 4 out of 5 in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe200 b:0.9 occ:1.00 FE1 E:FES200 0.0 0.9 1.0 S1 E:FES200 2.2 0.9 1.0 S2 E:FES200 2.2 0.7 1.0 SG E:CYS158 2.6 14.7 1.0 FE2 E:FES200 2.7 0.6 1.0 CB E:CYS139 3.3 16.4 1.0 SG E:CYS139 3.4 15.1 1.0 CB E:CYS158 3.7 15.9 1.0 CB E:CYS144 3.9 14.6 1.0 CB E:CYS160 4.0 14.8 1.0 SG E:CYS144 4.5 13.8 1.0 N E:CYS144 4.7 14.6 1.0 N E:HIS161 4.7 14.9 1.0 OG E:SER163 4.8 15.5 1.0 CB E:SER163 4.8 15.6 1.0 CA E:CYS144 4.8 14.7 1.0 CA E:CYS139 4.8 16.5 1.0 O E:CYS144 4.9 14.9 1.0 CB E:HIS141 5.0 15.3 1.0

Iron binding site 5 out of 5 in the Crystal Structure Analysis of Bovine BC1 with Azoxystrobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure Analysis of Bovine BC1 with Azoxystrobin within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe200 b:0.6 occ:1.00 FE2 E:FES200 0.0 0.6 1.0 S2 E:FES200 2.2 0.7 1.0 S1 E:FES200 2.2 0.9 1.0 FE1 E:FES200 2.7 0.9 1.0 ND1 E:HIS161 3.3 15.0 1.0 CG E:HIS161 3.4 14.9 1.0 CB E:HIS161 3.5 14.9 1.0 ND1 E:HIS141 3.5 14.9 1.0 CB E:CYS160 3.8 14.8 1.0 N E:HIS161 3.8 14.9 1.0 CD1 E:LEU142 4.0 13.2 1.0 CE1 E:HIS161 4.1 14.6 1.0 CD2 E:HIS161 4.2 14.8 1.0 CA E:HIS161 4.3 14.9 1.0 CG E:HIS141 4.4 15.2 1.0 CE1 E:HIS141 4.4 15.3 1.0 CB E:HIS141 4.4 15.3 1.0 NE2 E:HIS161 4.5 14.8 1.0 CB E:LEU142 4.5 14.7 1.0 CG E:LEU142 4.7 14.1 1.0 C E:CYS160 4.7 15.0 1.0 N E:LEU142 4.7 15.0 1.0 SG E:CYS158 4.8 14.7 1.0 SG E:CYS160 4.8 13.9 1.0 SG E:CYS144 4.8 13.8 1.0 CA E:CYS160 4.9 14.9 1.0 N E:GLY162 4.9 15.0 1.0

L.Esser, B.Quinn, Y.F.Li, M.Zhang, M.Elberry, L.Yu, C.A.Yu, D.Xia. Crystallographic Studies of Quinol Oxidation Site Inhibitors: A Modified Classification of Inhibitors For the Cytochrome Bc(1) Complex J.Mol.Biol. V. 341 281 2004.
ISSN: ISSN 0022-2836
PubMed: 15312779
DOI: 10.1016/J.JMB.2004.05.065