Atomistry » Iron » PDB 1kqj-1lfg » 1l0l
Atomistry »
  Iron »
    PDB 1kqj-1lfg »
      1l0l »

Iron in PDB 1l0l: Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone

Enzymatic activity of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone

All present enzymatic activity of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone:
1.10.2.2;

Protein crystallography data

The structure of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone, PDB code: 1l0l 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) 40.00 / 2.35
Space group I 41 2 2
Cell size a, b, c (Å), α, β, γ (°) 154.094, 154.094, 591.839, 90.00, 90.00, 90.00
R / Rfree (%) 25.9 / 30.6

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone (pdb code 1l0l). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 5 binding sites of Iron where determined in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone, PDB code: 1l0l:
Jump to Iron binding site number: 1; 2; 3; 4; 5;

Iron binding site 1 out of 5 in 1l0l

Go back to Iron Binding Sites List in 1l0l
Iron binding site 1 out of 5 in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe609

b:22.1
occ:1.00
FE C:HEM609 0.0 22.1 1.0
ND C:HEM609 2.0 25.6 1.0
NB C:HEM609 2.0 26.1 1.0
NC C:HEM609 2.0 23.6 1.0
NA C:HEM609 2.1 21.3 1.0
NE2 C:HIS196 2.2 15.8 1.0
NE2 C:HIS97 2.2 14.3 1.0
CD2 C:HIS97 2.9 21.6 1.0
CD2 C:HIS196 3.0 17.9 1.0
C1D C:HEM609 3.1 24.9 1.0
C1B C:HEM609 3.1 22.4 1.0
C4C C:HEM609 3.1 25.3 1.0
C4A C:HEM609 3.1 27.7 1.0
C4B C:HEM609 3.1 22.2 1.0
C4D C:HEM609 3.1 24.9 1.0
C1C C:HEM609 3.1 20.0 1.0
C1A C:HEM609 3.1 17.1 1.0
CE1 C:HIS196 3.2 13.3 1.0
CE1 C:HIS97 3.4 20.9 1.0
CHD C:HEM609 3.6 29.4 1.0
CHB C:HEM609 3.6 23.5 1.0
CHA C:HEM609 3.6 15.9 1.0
CHC C:HEM609 3.6 17.8 1.0
C2D C:HEM609 4.2 23.6 1.0
C2B C:HEM609 4.2 21.6 1.0
C3B C:HEM609 4.2 19.1 1.0
C3C C:HEM609 4.2 22.4 1.0
C2C C:HEM609 4.2 20.2 1.0
C3D C:HEM609 4.2 27.4 1.0
CG C:HIS97 4.2 20.4 1.0
CG C:HIS196 4.2 20.0 1.0
ND1 C:HIS196 4.3 20.6 1.0
C3A C:HEM609 4.4 27.0 1.0
C2A C:HEM609 4.4 23.7 1.0
ND1 C:HIS97 4.4 22.3 1.0

Iron binding site 2 out of 5 in 1l0l

Go back to Iron Binding Sites List in 1l0l
Iron binding site 2 out of 5 in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe610

b:20.5
occ:1.00
FE C:HEM610 0.0 20.5 1.0
NB C:HEM610 2.0 26.3 1.0
ND C:HEM610 2.0 23.6 1.0
NC C:HEM610 2.0 29.2 1.0
NE2 C:HIS182 2.1 16.6 1.0
NE2 C:HIS83 2.1 15.3 1.0
NA C:HEM610 2.1 22.0 1.0
CE1 C:HIS182 2.9 12.6 1.0
C1B C:HEM610 3.1 23.9 1.0
C4D C:HEM610 3.1 22.6 1.0
C4C C:HEM610 3.1 29.7 1.0
C4B C:HEM610 3.1 28.0 1.0
CE1 C:HIS83 3.1 15.6 1.0
C1C C:HEM610 3.1 27.2 1.0
C1D C:HEM610 3.1 25.0 1.0
C4A C:HEM610 3.1 23.7 1.0
C1A C:HEM610 3.1 18.0 1.0
CD2 C:HIS83 3.1 19.9 1.0
CD2 C:HIS182 3.2 13.7 1.0
CHB C:HEM610 3.6 24.9 1.0
CHA C:HEM610 3.6 19.2 1.0
CHD C:HEM610 3.6 26.9 1.0
CHC C:HEM610 3.6 27.1 1.0
ND1 C:HIS182 4.1 17.0 1.0
C3C C:HEM610 4.2 27.5 1.0
C2C C:HEM610 4.2 27.1 1.0
C2B C:HEM610 4.2 28.4 1.0
C3B C:HEM610 4.2 29.4 1.0
C3D C:HEM610 4.2 23.4 1.0
ND1 C:HIS83 4.2 16.3 1.0
C2D C:HEM610 4.2 25.2 1.0
CG C:HIS83 4.3 19.8 1.0
CG C:HIS182 4.3 17.3 1.0
C3A C:HEM610 4.4 19.7 1.0
C2A C:HEM610 4.4 16.9 1.0
CA C:GLY130 4.9 21.2 1.0
OE1 C:GLN44 4.9 24.3 1.0
CA C:GLY48 5.0 20.2 1.0

Iron binding site 3 out of 5 in 1l0l

Go back to Iron Binding Sites List in 1l0l
Iron binding site 3 out of 5 in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe242

b:15.1
occ:1.00
FE D:HEM242 0.0 15.1 1.0
NC D:HEM242 1.9 15.8 1.0
ND D:HEM242 2.0 14.8 1.0
NA D:HEM242 2.1 12.9 1.0
NB D:HEM242 2.1 15.4 1.0
NE2 D:HIS41 2.2 24.8 1.0
SD D:MET160 2.7 26.3 1.0
C4C D:HEM242 3.0 15.9 1.0
C1C D:HEM242 3.0 17.9 1.0
C1D D:HEM242 3.0 15.3 1.0
C4D D:HEM242 3.0 13.4 1.0
C1A D:HEM242 3.1 13.8 1.0
C4B D:HEM242 3.1 15.7 1.0
C4A D:HEM242 3.1 11.5 1.0
CE D:MET160 3.2 27.2 1.0
C1B D:HEM242 3.2 16.3 1.0
CE1 D:HIS41 3.2 26.3 1.0
CD2 D:HIS41 3.2 25.4 1.0
CHD D:HEM242 3.3 15.3 1.0
CHA D:HEM242 3.4 15.1 1.0
CHC D:HEM242 3.4 19.9 1.0
CHB D:HEM242 3.5 12.2 1.0
CG D:MET160 3.5 23.2 1.0
C3C D:HEM242 4.2 15.5 1.0
CB D:MET160 4.2 22.9 1.0
C2C D:HEM242 4.2 15.3 1.0
C2D D:HEM242 4.2 15.4 1.0
C3D D:HEM242 4.3 15.1 1.0
ND1 D:HIS41 4.3 27.4 1.0
C2A D:HEM242 4.3 9.9 1.0
C3A D:HEM242 4.3 9.9 1.0
C3B D:HEM242 4.3 15.4 1.0
CG D:HIS41 4.3 25.4 1.0
C2B D:HEM242 4.4 17.4 1.0

Iron binding site 4 out of 5 in 1l0l

Go back to Iron Binding Sites List in 1l0l
Iron binding site 4 out of 5 in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe197

b:20.7
occ:1.00
FE1 E:FES197 0.0 20.7 1.0
SG E:CYS158 2.0 17.0 1.0
S1 E:FES197 2.2 20.0 1.0
S2 E:FES197 2.2 21.5 1.0
SG E:CYS139 2.7 7.5 1.0
FE2 E:FES197 2.7 14.1 1.0
CB E:CYS158 3.4 18.6 1.0
CB E:CYS144 3.5 20.6 1.0
CB E:CYS139 3.7 11.4 1.0
O E:PRO159 4.0 25.5 1.0
O E:CYS144 4.1 19.4 1.0
SG E:CYS144 4.1 24.4 1.0
CB E:HIS141 4.1 13.7 1.0
N E:CYS144 4.5 17.9 1.0
ND1 E:HIS141 4.5 15.8 1.0
CA E:CYS144 4.5 18.8 1.0
NE2 E:HIS161 4.5 32.6 1.0
CB E:SER163 4.6 37.0 1.0
CA E:CYS158 4.6 19.8 1.0
CE1 E:HIS161 4.7 36.6 1.0
C E:CYS158 4.7 20.6 1.0
N E:LEU142 4.7 13.7 1.0
O E:CYS158 4.8 19.3 1.0
CB E:CYS160 4.8 27.4 1.0
CG E:HIS141 4.8 16.1 1.0
C E:CYS144 4.8 17.8 1.0
C E:PRO159 4.8 25.2 1.0

Iron binding site 5 out of 5 in 1l0l

Go back to Iron Binding Sites List in 1l0l
Iron binding site 5 out of 5 in the Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Structure of Bovine Mitochondrial Cytochrome BC1 Complex with A Bound Fungicide Famoxadone within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe197

b:14.1
occ:1.00
FE2 E:FES197 0.0 14.1 1.0
NE2 E:HIS161 2.1 32.6 1.0
CE1 E:HIS161 2.1 36.6 1.0
S1 E:FES197 2.2 20.0 1.0
S2 E:FES197 2.2 21.5 1.0
ND1 E:HIS141 2.4 15.8 1.0
FE1 E:FES197 2.7 20.7 1.0
CD2 E:HIS161 3.1 33.6 1.0
ND1 E:HIS161 3.1 37.5 1.0
CE1 E:HIS141 3.3 10.8 1.0
CG E:HIS141 3.3 16.1 1.0
CG E:HIS161 3.5 36.4 1.0
CB E:HIS141 3.6 13.7 1.0
CD1 E:LEU142 4.1 15.3 1.0
N E:LEU142 4.2 13.7 1.0
CG E:LEU142 4.3 17.4 1.0
NE2 E:HIS141 4.4 13.3 1.0
CD2 E:HIS141 4.4 15.8 1.0
CB E:LEU142 4.4 16.5 1.0
O E:PRO159 4.5 25.5 1.0
SG E:CYS158 4.5 17.0 1.0
SG E:CYS144 4.6 24.4 1.0
SG E:CYS139 4.7 7.5 1.0
CA E:HIS141 4.9 12.7 1.0
N E:GLY162 4.9 37.1 1.0
CB E:HIS161 4.9 34.5 1.0
C E:HIS141 4.9 12.5 1.0
CA E:LEU142 5.0 16.4 1.0
CB E:CYS144 5.0 20.6 1.0

Reference:

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
Page generated: Wed Jul 16 17:15:03 2025

Last articles

Zn in 1KH7
Zn in 1KH5
Zn in 1KH4
Zn in 1KFV
Zn in 1KFS
Zn in 1KEV
Zn in 1KFI
Zn in 1KBP
Zn in 1KEQ
Zn in 1KEI
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy