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Iron in PDB 29ye: Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites

Enzymatic activity of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites

All present enzymatic activity of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites:
7.1.1.8;

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites (pdb code 29ye). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 10 binding sites of Iron where determined in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites, PDB code: 29ye:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 10 in 29ye

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Iron binding site 1 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:123.5
occ:1.00
 FE1 A:FES501 0.0 123.5 1.0
S1 A:FES501 2.2 106.6 1.0
S2 A:FES501 2.2 102.3 1.0
SG A:CYS155 2.3 103.5 1.0
SG A:CYS135 2.3 103.6 1.0
FE2 A:FES501 2.7 116.1 1.0
CB A:CYS135 3.2 94.1 1.0
CB A:CYS155 3.4 94.2 1.0
CB A:HIS137 4.0 89.8 1.0
ND1 A:HIS137 4.3 95.8 1.0
CB A:CYS140 4.4 92.8 1.0
OG A:SER160 4.4 102.2 1.0
N A:LEU138 4.6 89.8 1.0
CB A:CYS157 4.6 103.7 1.0
N A:CYS140 4.6 92.0 1.0
ND1 A:HIS158 4.6 104.6 1.0
CA A:CYS135 4.6 89.3 1.0
CG A:HIS137 4.7 94.3 1.0
CA A:CYS155 4.8 94.0 1.0
N A:HIS158 4.8 100.0 1.0
N A:HIS137 4.8 95.2 1.0
CB A:SER160 4.9 99.7 1.0
CA A:HIS137 4.9 90.4 1.0
SG A:CYS140 5.0 123.6 1.0
CA A:CYS140 5.0 88.8 1.0

Iron binding site 2 out of 10 in 29ye

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Iron binding site 2 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:116.1
occ:1.00
 FE2 A:FES501 0.0 116.1 1.0
S1 A:FES501 2.2 106.6 1.0
S2 A:FES501 2.2 102.3 1.0
ND1 A:HIS158 2.2 104.6 1.0
ND1 A:HIS137 2.3 95.8 1.0
FE1 A:FES501 2.7 123.5 1.0
CG A:HIS158 3.1 100.8 1.0
CE1 A:HIS137 3.2 93.4 1.0
CE1 A:HIS158 3.2 101.2 1.0
CG A:HIS137 3.3 94.3 1.0
CB A:HIS158 3.3 96.5 1.0
CB A:HIS137 3.6 89.8 1.0
N A:HIS158 3.8 100.0 1.0
CB A:CYS157 4.1 103.7 1.0
CA A:HIS158 4.1 97.6 1.0
N A:LEU138 4.3 89.8 1.0
CD2 A:HIS158 4.3 102.3 1.0
NE2 A:HIS158 4.3 101.6 1.0
NE2 A:HIS137 4.3 90.4 1.0
SG A:CYS155 4.3 103.5 1.0
CB A:LEU138 4.4 89.3 1.0
CD2 A:HIS137 4.4 93.0 1.0
C A:CYS157 4.5 101.1 1.0
SG A:CYS135 4.5 103.6 1.0
CG A:LEU138 4.7 87.0 1.0
CD1 A:LEU138 4.7 86.7 1.0
CA A:HIS137 4.8 90.4 1.0
C A:HIS137 4.8 91.1 1.0
C A:HIS158 4.9 102.1 1.0
CA A:LEU138 4.9 86.3 1.0
CA A:CYS157 4.9 100.1 1.0
CG A:PRO172 5.0 96.3 1.0

Iron binding site 3 out of 10 in 29ye

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Iron binding site 3 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:93.0
occ:1.00
 FE B:HEM501 0.0 93.0 1.0
NC B:HEM501 2.0 77.2 1.0
ND B:HEM501 2.0 75.9 1.0
NA B:HEM501 2.1 74.1 1.0
NB B:HEM501 2.1 75.9 1.0
NE2 B:HIS97 2.3 74.1 1.0
NE2 B:HIS198 2.3 74.5 1.0
C1C B:HEM501 3.1 74.5 1.0
C4D B:HEM501 3.1 75.7 1.0
C1A B:HEM501 3.1 72.2 1.0
C4B B:HEM501 3.1 73.1 1.0
C4C B:HEM501 3.1 76.3 1.0
C1D B:HEM501 3.1 73.0 1.0
C1B B:HEM501 3.1 72.0 1.0
C4A B:HEM501 3.1 72.6 1.0
CE1 B:HIS198 3.1 73.1 1.0
CE1 B:HIS97 3.2 72.0 1.0
CD2 B:HIS97 3.3 74.1 1.0
CD2 B:HIS198 3.3 76.9 1.0
CHC B:HEM501 3.4 71.9 1.0
CHA B:HEM501 3.4 71.7 1.0
CHD B:HEM501 3.4 72.0 1.0
CHB B:HEM501 3.5 71.2 1.0
C2C B:HEM501 4.3 73.0 1.0
C3D B:HEM501 4.3 77.7 1.0
C3C B:HEM501 4.3 74.5 1.0
C3B B:HEM501 4.3 74.7 1.0
C2A B:HEM501 4.3 71.1 1.0
C2B B:HEM501 4.3 73.4 1.0
C2D B:HEM501 4.3 74.8 1.0
C3A B:HEM501 4.3 71.5 1.0
ND1 B:HIS198 4.3 78.7 1.0
ND1 B:HIS97 4.3 76.2 1.0
CG B:HIS97 4.4 74.5 1.0
CG B:HIS198 4.4 80.6 1.0

Iron binding site 4 out of 10 in 29ye

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Iron binding site 4 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:101.6
occ:1.00
 FE B:HEM502 0.0 101.6 1.0
NB B:HEM502 2.0 82.7 1.0
ND B:HEM502 2.0 83.9 1.0
NA B:HEM502 2.1 85.6 1.0
NC B:HEM502 2.1 82.2 1.0
NE2 B:HIS212 2.3 82.2 1.0
NE2 B:HIS111 2.4 82.4 1.0
C1D B:HEM502 3.1 82.3 1.0
C1B B:HEM502 3.1 80.4 1.0
C4C B:HEM502 3.1 78.5 1.0
C4A B:HEM502 3.1 82.8 1.0
C4B B:HEM502 3.1 78.8 1.0
C1A B:HEM502 3.1 84.8 1.0
C4D B:HEM502 3.1 80.3 1.0
C1C B:HEM502 3.1 76.9 1.0
CD2 B:HIS212 3.2 79.5 1.0
CD2 B:HIS111 3.2 80.7 1.0
CE1 B:HIS212 3.4 83.5 1.0
CHD B:HEM502 3.4 79.2 1.0
CHB B:HEM502 3.4 78.7 1.0
CE1 B:HIS111 3.4 84.5 1.0
CHC B:HEM502 3.4 75.9 1.0
CHA B:HEM502 3.5 81.0 1.0
C2D B:HEM502 4.3 81.3 1.0
C2B B:HEM502 4.3 79.1 1.0
C3A B:HEM502 4.3 84.5 1.0
C3C B:HEM502 4.3 78.8 1.0
C3B B:HEM502 4.3 77.8 1.0
C2A B:HEM502 4.3 86.3 1.0
C3D B:HEM502 4.3 82.1 1.0
C2C B:HEM502 4.3 76.5 1.0
CG B:HIS212 4.4 83.6 1.0
CG B:HIS111 4.4 81.5 1.0
ND1 B:HIS212 4.4 87.4 1.0
ND1 B:HIS111 4.5 86.6 1.0

Iron binding site 5 out of 10 in 29ye

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Iron binding site 5 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:114.4
occ:1.00
 FE C:HEC501 0.0 114.4 1.0
NA C:HEC501 2.0 96.5 1.0
NC C:HEC501 2.1 97.0 1.0
NB C:HEC501 2.1 97.7 1.0
ND C:HEC501 2.1 99.4 1.0
NE2 C:HIS38 2.2 93.7 1.0
SD C:MET183 2.4 100.9 1.0
CE1 C:HIS38 3.0 91.4 1.0
C1A C:HEC501 3.1 95.1 1.0
C1C C:HEC501 3.1 93.3 1.0
C4C C:HEC501 3.1 97.7 1.0
C4D C:HEC501 3.1 96.4 1.0
C4B C:HEC501 3.1 95.4 1.0
C4A C:HEC501 3.1 92.6 1.0
C1D C:HEC501 3.1 97.8 1.0
C1B C:HEC501 3.1 94.3 1.0
CD2 C:HIS38 3.4 94.3 1.0
CHA C:HEC501 3.4 96.1 1.0
CHC C:HEC501 3.4 92.5 1.0
CHD C:HEC501 3.4 98.5 1.0
CE C:MET183 3.5 98.1 1.0
CHB C:HEC501 3.5 92.7 1.0
CG C:MET183 3.5 98.8 1.0
ND1 C:HIS38 4.2 88.8 1.0
C2C C:HEC501 4.3 96.1 1.0
C2A C:HEC501 4.3 92.9 1.0
C3C C:HEC501 4.3 100.5 1.0
CB C:MET183 4.3 100.7 1.0
C3A C:HEC501 4.3 90.4 1.0
C3B C:HEC501 4.3 93.4 1.0
C2B C:HEC501 4.3 91.0 1.0
C3D C:HEC501 4.3 96.9 1.0
C2D C:HEC501 4.3 96.6 1.0
CG C:HIS38 4.4 91.8 1.0

Iron binding site 6 out of 10 in 29ye

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Iron binding site 6 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:123.0
occ:1.00
 FE1 D:FES501 0.0 123.0 1.0
S2 D:FES501 2.2 101.9 1.0
S1 D:FES501 2.2 107.0 1.0
SG D:CYS155 2.3 103.2 1.0
SG D:CYS135 2.3 103.5 1.0
FE2 D:FES501 2.7 115.8 1.0
CB D:CYS135 3.2 93.8 1.0
CB D:CYS155 3.4 94.4 1.0
CB D:HIS137 4.0 89.8 1.0
ND1 D:HIS137 4.3 95.5 1.0
CB D:CYS140 4.4 93.2 1.0
OG D:SER160 4.4 102.0 1.0
N D:LEU138 4.6 89.9 1.0
CB D:CYS157 4.6 103.3 1.0
N D:CYS140 4.6 92.2 1.0
ND1 D:HIS158 4.6 104.5 1.0
CA D:CYS135 4.6 89.2 1.0
CG D:HIS137 4.7 94.2 1.0
CA D:CYS155 4.8 94.3 1.0
N D:HIS158 4.8 99.8 1.0
N D:HIS137 4.8 95.5 1.0
CB D:SER160 4.9 99.6 1.0
CA D:HIS137 4.9 90.6 1.0
SG D:CYS140 5.0 123.7 1.0
CA D:CYS140 5.0 89.3 1.0

Iron binding site 7 out of 10 in 29ye

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Iron binding site 7 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:115.8
occ:1.00
 FE2 D:FES501 0.0 115.8 1.0
S2 D:FES501 2.2 101.9 1.0
S1 D:FES501 2.2 107.0 1.0
ND1 D:HIS158 2.2 104.5 1.0
ND1 D:HIS137 2.3 95.5 1.0
FE1 D:FES501 2.7 123.0 1.0
CG D:HIS158 3.1 100.6 1.0
CE1 D:HIS137 3.2 92.9 1.0
CE1 D:HIS158 3.2 101.1 1.0
CG D:HIS137 3.3 94.2 1.0
CB D:HIS158 3.3 96.3 1.0
CB D:HIS137 3.6 89.8 1.0
N D:HIS158 3.8 99.8 1.0
CB D:CYS157 4.1 103.3 1.0
CA D:HIS158 4.1 97.4 1.0
N D:LEU138 4.2 89.9 1.0
CD2 D:HIS158 4.3 102.2 1.0
NE2 D:HIS158 4.3 101.3 1.0
NE2 D:HIS137 4.3 90.2 1.0
SG D:CYS155 4.3 103.2 1.0
CB D:LEU138 4.3 89.3 1.0
CD2 D:HIS137 4.4 92.9 1.0
C D:CYS157 4.5 101.1 1.0
SG D:CYS135 4.5 103.5 1.0
CG D:LEU138 4.7 87.3 1.0
CD1 D:LEU138 4.7 86.9 1.0
CA D:HIS137 4.8 90.6 1.0
C D:HIS137 4.8 91.4 1.0
C D:HIS158 4.9 101.8 1.0
CA D:LEU138 4.9 86.6 1.0
CA D:CYS157 4.9 99.6 1.0
CG D:PRO172 5.0 96.2 1.0

Iron binding site 8 out of 10 in 29ye

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Iron binding site 8 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe502

b:93.0
occ:1.00
 FE E:HEM502 0.0 93.0 1.0
NC E:HEM502 2.0 77.4 1.0
ND E:HEM502 2.0 76.2 1.0
NA E:HEM502 2.1 74.1 1.0
NB E:HEM502 2.1 76.0 1.0
NE2 E:HIS97 2.3 74.4 1.0
NE2 E:HIS198 2.3 74.5 1.0
C1C E:HEM502 3.1 74.9 1.0
C4D E:HEM502 3.1 76.1 1.0
C1A E:HEM502 3.1 72.6 1.0
C4B E:HEM502 3.1 73.2 1.0
C4C E:HEM502 3.1 76.3 1.0
C1D E:HEM502 3.1 73.2 1.0
C1B E:HEM502 3.1 72.2 1.0
C4A E:HEM502 3.1 72.7 1.0
CE1 E:HIS198 3.1 73.1 1.0
CE1 E:HIS97 3.2 72.4 1.0
CD2 E:HIS97 3.3 74.3 1.0
CD2 E:HIS198 3.3 76.8 1.0
CHC E:HEM502 3.4 72.1 1.0
CHA E:HEM502 3.4 72.1 1.0
CHD E:HEM502 3.4 72.1 1.0
CHB E:HEM502 3.5 71.4 1.0
C2C E:HEM502 4.3 73.5 1.0
C3D E:HEM502 4.3 77.9 1.0
C3C E:HEM502 4.3 74.6 1.0
C3B E:HEM502 4.3 74.9 1.0
C2A E:HEM502 4.3 71.3 1.0
C2B E:HEM502 4.3 73.4 1.0
C2D E:HEM502 4.3 75.1 1.0
C3A E:HEM502 4.3 71.7 1.0
ND1 E:HIS198 4.3 78.8 1.0
ND1 E:HIS97 4.3 76.4 1.0
CG E:HIS97 4.4 74.7 1.0
CG E:HIS198 4.4 80.7 1.0

Iron binding site 9 out of 10 in 29ye

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Iron binding site 9 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe503

b:101.3
occ:1.00
 FE E:HEM503 0.0 101.3 1.0
NB E:HEM503 2.0 81.9 1.0
ND E:HEM503 2.0 83.9 1.0
NA E:HEM503 2.1 85.3 1.0
NC E:HEM503 2.1 81.7 1.0
NE2 E:HIS212 2.3 82.0 1.0
NE2 E:HIS111 2.4 82.3 1.0
C1D E:HEM503 3.1 82.2 1.0
C1B E:HEM503 3.1 79.7 1.0
C4C E:HEM503 3.1 78.1 1.0
C4A E:HEM503 3.1 82.4 1.0
C4B E:HEM503 3.1 78.3 1.0
C1A E:HEM503 3.1 84.1 1.0
C4D E:HEM503 3.1 80.0 1.0
C1C E:HEM503 3.1 76.7 1.0
CD2 E:HIS212 3.2 79.3 1.0
CD2 E:HIS111 3.2 80.6 1.0
CE1 E:HIS212 3.4 83.2 1.0
CHD E:HEM503 3.4 78.9 1.0
CHB E:HEM503 3.4 78.3 1.0
CE1 E:HIS111 3.4 84.2 1.0
CHC E:HEM503 3.4 75.9 1.0
CHA E:HEM503 3.5 80.2 1.0
C2D E:HEM503 4.3 80.9 1.0
C2B E:HEM503 4.3 78.4 1.0
C3A E:HEM503 4.3 84.4 1.0
C3C E:HEM503 4.3 78.3 1.0
C3B E:HEM503 4.3 77.3 1.0
C2A E:HEM503 4.3 86.0 1.0
C3D E:HEM503 4.3 81.8 1.0
C2C E:HEM503 4.3 76.3 1.0
CG E:HIS212 4.4 83.2 1.0
CG E:HIS111 4.4 81.4 1.0
ND1 E:HIS212 4.4 87.1 1.0
ND1 E:HIS111 4.5 86.7 1.0

Iron binding site 10 out of 10 in 29ye

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Iron binding site 10 out of 10 in the Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Cryo-Em Structure of +2ALA Insertion Mutant of Rhodobacter Capsulatus Cytochrome BC1 Dimer at 2.41 A with Quinone in Quinone Oxidation and Reduction Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:114.7
occ:1.00
 FE F:HEC501 0.0 114.7 1.0
NA F:HEC501 2.0 96.5 1.0
NC F:HEC501 2.1 97.4 1.0
NB F:HEC501 2.1 98.0 1.0
ND F:HEC501 2.1 99.2 1.0
NE2 F:HIS38 2.2 93.9 1.0
SD F:MET183 2.4 101.1 1.0
CE1 F:HIS38 3.0 91.4 1.0
C1A F:HEC501 3.1 94.9 1.0
C1C F:HEC501 3.1 93.7 1.0
C4C F:HEC501 3.1 97.9 1.0
C4D F:HEC501 3.1 96.3 1.0
C4B F:HEC501 3.1 95.8 1.0
C4A F:HEC501 3.1 92.9 1.0
C1D F:HEC501 3.1 97.8 1.0
C1B F:HEC501 3.1 94.5 1.0
CD2 F:HIS38 3.4 94.6 1.0
CHA F:HEC501 3.4 96.1 1.0
CHC F:HEC501 3.4 92.9 1.0
CHD F:HEC501 3.4 98.5 1.0
CE F:MET183 3.5 98.7 1.0
CHB F:HEC501 3.5 92.9 1.0
CG F:MET183 3.5 98.8 1.0
ND1 F:HIS38 4.2 88.8 1.0
C2C F:HEC501 4.3 96.3 1.0
C2A F:HEC501 4.3 92.8 1.0
C3C F:HEC501 4.3 100.3 1.0
CB F:MET183 4.3 100.4 1.0
C3A F:HEC501 4.3 90.6 1.0
C3B F:HEC501 4.3 93.8 1.0
C2B F:HEC501 4.3 91.2 1.0
C3D F:HEC501 4.3 97.1 1.0
C2D F:HEC501 4.3 96.8 1.0
CG F:HIS38 4.4 92.2 1.0

Reference:

R.Pietras, A.Wojcik-Augustyn, B.Mielecki, M.Sarewicz, M.Jaciuk, L.Koziej, S.Glatt, A.Osyczka. Distinct Ubiquinone Binding at the Oxidation and Reduction Sites of Cytochrome Bc 1. Proc.Natl.Acad.Sci.Usa V. 123 42123 2026.
ISSN: ESSN 1091-6490
PubMed: 42679026
DOI: 10.1073/PNAS.2618242123
Page generated: Sun Oct 4 09:43:26 2026

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