Iron in PDB 1l0n: Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex

All present enzymatic activity of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex:
1.10.2.2;

The structure of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex, PDB code: 1l0n was solved by X.Gao, X.Wen, C.A.Yu, L.Esser, S.Tsao, B.Quinn, L.Zhang, L.Yu, D.Xia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.99 / 2.60
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	153.828, 153.828, 596.671, 90.00, 90.00, 90.00
R / Rfree (%)	26.1 / 29.7

The binding sites of Iron atom in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex (pdb code 1l0n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex, PDB code: 1l0n:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe381 b:76.2 occ:1.00 FE C:HEM381 0.0 76.2 1.0 NA C:HEM381 1.9 71.7 1.0 NC C:HEM381 2.0 68.5 1.0 ND C:HEM381 2.0 68.4 1.0 NE2 C:HIS196 2.1 23.1 1.0 NB C:HEM381 2.1 82.8 1.0 NE2 C:HIS97 2.3 42.4 1.0 C4C C:HEM381 2.9 73.7 1.0 C4A C:HEM381 2.9 79.1 1.0 CD2 C:HIS97 2.9 51.3 1.0 CD2 C:HIS196 2.9 30.0 1.0 C1D C:HEM381 3.0 71.0 1.0 C1A C:HEM381 3.0 78.3 1.0 C1B C:HEM381 3.0 82.2 1.0 C4D C:HEM381 3.1 72.6 1.0 C1C C:HEM381 3.1 81.9 1.0 CE1 C:HIS196 3.2 32.7 1.0 CHD C:HEM381 3.2 75.3 1.0 C4B C:HEM381 3.2 85.7 1.0 CHB C:HEM381 3.3 75.5 1.0 CHA C:HEM381 3.4 80.3 1.0 CE1 C:HIS97 3.4 56.6 1.0 CHC C:HEM381 3.6 85.1 1.0 C3A C:HEM381 4.1 82.4 1.0 CG C:HIS196 4.1 33.9 1.0 C3C C:HEM381 4.1 79.4 1.0 C2A C:HEM381 4.2 78.1 1.0 CG C:HIS97 4.2 41.9 1.0 ND1 C:HIS196 4.2 39.7 1.0 C2D C:HEM381 4.2 68.0 1.0 C3D C:HEM381 4.3 61.1 1.0 C2C C:HEM381 4.3 82.1 1.0 C2B C:HEM381 4.3 86.7 1.0 ND1 C:HIS97 4.4 42.6 1.0 C3B C:HEM381 4.4 88.1 1.0

Iron binding site 2 out of 5 in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe382 b:0.7 occ:1.00 FE C:HEM382 0.0 0.7 1.0 NE2 C:HIS83 2.0 26.0 1.0 NE2 C:HIS182 2.0 28.5 1.0 NC C:HEM382 2.0 0.2 1.0 NA C:HEM382 2.1 0.5 1.0 ND C:HEM382 2.1 0.9 1.0 NB C:HEM382 2.1 0.0 1.0 CE1 C:HIS83 2.9 27.6 1.0 CE1 C:HIS182 2.9 30.2 1.0 C4C C:HEM382 3.0 0.9 1.0 CD2 C:HIS182 3.1 36.2 1.0 CD2 C:HIS83 3.1 27.0 1.0 C1D C:HEM382 3.1 0.1 1.0 C1C C:HEM382 3.1 0.1 1.0 C1A C:HEM382 3.1 0.8 1.0 C4D C:HEM382 3.1 0.4 1.0 C4A C:HEM382 3.1 0.2 1.0 C4B C:HEM382 3.1 0.7 1.0 C1B C:HEM382 3.2 0.5 1.0 CHD C:HEM382 3.4 0.0 1.0 CHA C:HEM382 3.4 0.7 1.0 CHC C:HEM382 3.5 0.2 1.0 CHB C:HEM382 3.5 0.4 1.0 ND1 C:HIS83 4.0 40.9 1.0 ND1 C:HIS182 4.0 41.5 1.0 CG C:HIS83 4.1 29.3 1.0 CG C:HIS182 4.1 38.7 1.0 C3C C:HEM382 4.2 0.8 1.0 C2C C:HEM382 4.3 0.5 1.0 NE2 C:GLN44 4.3 73.8 1.0 C2A C:HEM382 4.3 0.4 1.0 C2D C:HEM382 4.3 0.6 1.0 C3A C:HEM382 4.3 0.8 1.0 C3D C:HEM382 4.3 0.8 1.0 C3B C:HEM382 4.4 0.2 1.0 C2B C:HEM382 4.4 0.7 1.0 CA C:GLY130 4.8 44.4 1.0

Iron binding site 3 out of 5 in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe242 b:0.8 occ:1.00 FE D:HEM242 0.0 0.8 1.0 NB D:HEM242 2.0 0.1 1.0 NA D:HEM242 2.0 94.7 1.0 NC D:HEM242 2.0 99.7 1.0 ND D:HEM242 2.2 93.8 1.0 NE2 D:HIS41 2.3 34.2 1.0 SD D:MET160 2.5 45.5 1.0 C1C D:HEM242 2.9 0.5 1.0 C4B D:HEM242 3.0 0.5 1.0 C4A D:HEM242 3.0 98.7 1.0 C1B D:HEM242 3.0 0.1 1.0 C1A D:HEM242 3.0 99.6 1.0 C4C D:HEM242 3.0 0.9 1.0 CG D:MET160 3.1 39.9 1.0 C1D D:HEM242 3.2 95.4 1.0 C4D D:HEM242 3.2 97.3 1.0 CD2 D:HIS41 3.2 34.0 1.0 CE1 D:HIS41 3.3 30.3 1.0 CHC D:HEM242 3.3 1.0 1.0 CHB D:HEM242 3.3 97.6 1.0 CHA D:HEM242 3.5 99.6 1.0 CHD D:HEM242 3.5 99.8 1.0 CE D:MET160 4.1 50.6 1.0 CB D:MET160 4.2 38.6 1.0 C2C D:HEM242 4.2 0.5 1.0 C3B D:HEM242 4.2 0.3 1.0 C3A D:HEM242 4.2 1.0 1.0 C3C D:HEM242 4.2 0.1 1.0 C2B D:HEM242 4.2 0.8 1.0 C2A D:HEM242 4.2 0.9 1.0 ND1 D:HIS41 4.3 32.8 1.0 CG D:HIS41 4.3 35.0 1.0 C2D D:HEM242 4.4 94.9 1.0 C3D D:HEM242 4.4 95.9 1.0

Iron binding site 4 out of 5 in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe197 b:51.6 occ:1.00 FE1 E:FES197 0.0 51.6 1.0 S1 E:FES197 2.2 47.8 1.0 S2 E:FES197 2.2 52.6 1.0 FE2 E:FES197 2.7 50.8 1.0 SG E:CYS144 2.8 25.9 1.0 O E:PRO159 3.1 22.9 1.0 O E:CYS158 3.3 24.2 1.0 SG E:CYS160 3.5 28.4 1.0 CB E:CYS160 3.6 22.6 1.0 SG E:CYS139 3.7 19.0 1.0 SG E:CYS158 3.7 21.7 1.0 CB E:SER163 3.8 19.9 1.0 C E:PRO159 4.0 23.0 1.0 C E:CYS158 4.2 24.1 1.0 CB E:CYS144 4.5 19.4 1.0 CB E:CYS158 4.5 24.1 1.0 N E:CYS160 4.6 22.7 1.0 OG E:SER163 4.7 19.2 1.0 N E:HIS161 4.7 21.9 1.0 C E:GLY162 4.7 20.4 1.0 N E:SER163 4.7 20.1 1.0 CA E:CYS160 4.7 22.5 1.0 N E:GLY162 4.7 21.0 1.0 CB E:CYS139 4.7 20.0 1.0 ND1 E:HIS141 4.8 14.5 1.0 CB E:PRO175 4.8 18.1 1.0 O E:GLY162 4.8 20.4 1.0 N E:PRO159 4.9 23.9 1.0 CA E:SER163 4.9 19.9 1.0 CA E:PRO159 4.9 23.4 1.0 CA E:CYS158 5.0 24.2 1.0

Iron binding site 5 out of 5 in the Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Native Structure of Bovine Mitochondrial Cytochrome BC1 Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe197 b:50.8 occ:1.00 FE2 E:FES197 0.0 50.8 1.0 S1 E:FES197 2.2 47.8 1.0 S2 E:FES197 2.2 52.6 1.0 FE1 E:FES197 2.7 51.6 1.0 ND1 E:HIS141 3.3 14.5 1.0 CE1 E:HIS161 3.3 24.4 1.0 ND1 E:HIS161 3.4 24.2 1.0 NE2 E:HIS161 3.4 24.5 1.0 CD1 E:LEU142 3.5 8.9 1.0 CB E:CYS160 3.5 22.6 1.0 CG E:HIS161 3.6 23.9 1.0 CD2 E:HIS161 3.6 24.0 1.0 CE1 E:HIS141 3.7 13.8 1.0 CG E:LEU142 3.9 12.0 1.0 SG E:CYS160 3.9 28.4 1.0 CG E:HIS141 4.2 16.8 1.0 N E:HIS161 4.3 21.9 1.0 O E:PRO159 4.3 22.9 1.0 CB E:HIS161 4.4 21.8 1.0 CB E:LEU142 4.4 18.1 1.0 SG E:CYS144 4.6 25.9 1.0 CB E:PRO175 4.6 18.1 1.0 CB E:HIS141 4.7 18.3 1.0 NE2 E:HIS141 4.7 14.8 1.0 CA E:CYS160 4.9 22.5 1.0 N E:LEU142 4.9 18.3 1.0 N E:GLY162 5.0 21.0 1.0 CA E:HIS161 5.0 21.7 1.0

X.Gao, X.Wen, C.A.Yu, L.Esser, S.Tsao, B.Quinn, L.Zhang, L.Yu, D.Xia. The Crystal Structure of Mitochondrial Cytochrome BC1 in Complex with Famoxadone: the Role of Aromatic-Aromatic Interaction in Inhibition Biochemistry V. 41 11692 2003.
ISSN: ISSN 0006-2960
PubMed: 12269811
DOI: 10.1021/BI026252P