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Iron in PDB 29yc: Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position

Enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position

All present enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position:
7.1.1.8;

Iron Binding Sites:

The binding sites of Iron atom in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position (pdb code 29yc). 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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position, PDB code: 29yc:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 10 in 29yc

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Iron binding site 1 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:113.5
occ:1.00
 FE1 A:FES501 0.0 113.5 1.0
S1 A:FES501 2.2 101.4 1.0
S2 A:FES501 2.2 104.5 1.0
SG A:CYS153 2.3 92.7 1.0
SG A:CYS133 2.3 91.1 1.0
FE2 A:FES501 2.7 109.6 1.0
CB A:CYS133 3.2 76.9 1.0
CB A:CYS153 3.4 83.9 1.0
CB A:HIS135 3.9 84.6 1.0
CB A:CYS138 4.1 98.4 1.0
ND1 A:HIS135 4.3 88.5 1.0
CB A:CYS155 4.4 92.4 1.0
OG A:SER158 4.5 90.6 1.0
CG A:HIS135 4.6 84.8 1.0
N A:LEU136 4.6 84.9 1.0
N A:CYS138 4.6 92.5 1.0
ND1 A:HIS156 4.6 93.0 1.0
CA A:CYS133 4.7 73.2 1.0
CA A:CYS153 4.8 84.1 1.0
CB A:SER158 4.8 89.5 1.0
N A:HIS135 4.8 83.0 1.0
CA A:CYS138 4.8 87.8 1.0
SG A:CYS138 4.9 147.9 1.0
O A:CYS138 4.9 89.9 1.0
N A:HIS156 4.9 90.2 1.0
CA A:HIS135 4.9 80.4 1.0

Iron binding site 2 out of 10 in 29yc

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Iron binding site 2 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:109.6
occ:1.00
 FE2 A:FES501 0.0 109.6 1.0
ND1 A:HIS156 2.1 93.0 1.0
ND1 A:HIS135 2.1 88.5 1.0
S1 A:FES501 2.2 101.4 1.0
S2 A:FES501 2.2 104.5 1.0
FE1 A:FES501 2.7 113.5 1.0
CG A:HIS156 3.0 88.5 1.0
CE1 A:HIS135 3.1 83.2 1.0
CG A:HIS135 3.2 84.8 1.0
CE1 A:HIS156 3.2 92.7 1.0
CB A:HIS156 3.2 87.5 1.0
CB A:HIS135 3.5 84.6 1.0
N A:HIS156 3.7 90.2 1.0
CB A:CYS155 4.1 92.4 1.0
CA A:HIS156 4.1 86.9 1.0
CD2 A:HIS156 4.1 84.8 1.0
NE2 A:HIS156 4.2 89.9 1.0
NE2 A:HIS135 4.2 82.2 1.0
CD2 A:HIS135 4.3 84.0 1.0
SG A:CYS153 4.3 92.7 1.0
C A:CYS155 4.4 90.9 1.0
N A:LEU136 4.5 84.9 1.0
SG A:CYS133 4.5 91.1 1.0
CB A:LEU136 4.7 85.7 1.0
CA A:CYS155 4.8 88.8 1.0
OG A:SER158 4.8 90.6 1.0
CA A:HIS135 4.8 80.4 1.0
C A:HIS156 4.9 91.7 1.0
CG A:PRO170 4.9 80.1 1.0
C A:HIS135 4.9 85.2 1.0
CG A:LEU136 5.0 88.3 1.0

Iron binding site 3 out of 10 in 29yc

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Iron binding site 3 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:89.3
occ:1.00
 FE B:HEM501 0.0 89.3 1.0
ND B:HEM501 2.0 65.4 1.0
NC B:HEM501 2.0 68.4 1.0
NA B:HEM501 2.0 64.3 1.0
NB B:HEM501 2.0 64.2 1.0
NE2 B:HIS198 2.2 64.3 1.0
NE2 B:HIS97 2.2 64.9 1.0
CE1 B:HIS198 3.0 60.2 1.0
C4D B:HEM501 3.0 63.7 1.0
C4C B:HEM501 3.0 66.9 1.0
C1D B:HEM501 3.0 66.0 1.0
C1C B:HEM501 3.1 64.7 1.0
C4B B:HEM501 3.1 62.1 1.0
C1A B:HEM501 3.1 59.6 1.0
C1B B:HEM501 3.1 62.7 1.0
C4A B:HEM501 3.1 61.0 1.0
CE1 B:HIS97 3.1 62.7 1.0
CD2 B:HIS97 3.3 61.7 1.0
CD2 B:HIS198 3.3 63.0 1.0
CHC B:HEM501 3.4 61.4 1.0
CHD B:HEM501 3.4 67.1 1.0
CHA B:HEM501 3.4 60.4 1.0
CHB B:HEM501 3.4 58.1 1.0
ND1 B:HIS198 4.2 63.2 1.0
C3D B:HEM501 4.3 65.9 1.0
C2D B:HEM501 4.3 64.1 1.0
C3C B:HEM501 4.3 64.2 1.0
C2C B:HEM501 4.3 64.9 1.0
C3B B:HEM501 4.3 64.3 1.0
C2A B:HEM501 4.3 62.9 1.0
C3A B:HEM501 4.3 63.2 1.0
C2B B:HEM501 4.3 66.0 1.0
ND1 B:HIS97 4.3 63.4 1.0
CG B:HIS198 4.4 64.6 1.0
CG B:HIS97 4.4 64.2 1.0

Iron binding site 4 out of 10 in 29yc

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Iron binding site 4 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:90.3
occ:1.00
 FE B:HEM502 0.0 90.3 1.0
ND B:HEM502 2.0 72.9 1.0
NA B:HEM502 2.0 75.0 1.0
NB B:HEM502 2.0 72.4 1.0
NC B:HEM502 2.0 71.2 1.0
NE2 B:HIS212 2.3 67.9 1.0
NE2 B:HIS111 2.3 71.3 1.0
C4C B:HEM502 3.0 65.9 1.0
C4D B:HEM502 3.0 69.8 1.0
C1D B:HEM502 3.0 69.3 1.0
C1C B:HEM502 3.0 70.4 1.0
C4A B:HEM502 3.0 75.8 1.0
C1A B:HEM502 3.0 68.9 1.0
C1B B:HEM502 3.0 66.1 1.0
C4B B:HEM502 3.1 66.7 1.0
CD2 B:HIS111 3.1 69.3 1.0
CD2 B:HIS212 3.2 65.2 1.0
CE1 B:HIS212 3.3 69.9 1.0
CHD B:HEM502 3.4 65.2 1.0
CHB B:HEM502 3.4 67.1 1.0
CHA B:HEM502 3.4 69.0 1.0
CHC B:HEM502 3.4 63.7 1.0
CE1 B:HIS111 3.5 73.2 1.0
C3C B:HEM502 4.2 67.9 1.0
C2C B:HEM502 4.2 68.0 1.0
C3D B:HEM502 4.3 68.7 1.0
C2D B:HEM502 4.3 72.1 1.0
C2A B:HEM502 4.3 72.3 1.0
C3A B:HEM502 4.3 74.2 1.0
C2B B:HEM502 4.3 60.8 1.0
C3B B:HEM502 4.3 62.5 1.0
CG B:HIS111 4.3 70.7 1.0
ND1 B:HIS212 4.3 76.0 1.0
CG B:HIS212 4.4 71.7 1.0
ND1 B:HIS111 4.5 78.5 1.0

Iron binding site 5 out of 10 in 29yc

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Iron binding site 5 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:94.4
occ:1.00
 FE C:HEC501 0.0 94.4 1.0
NA C:HEC501 2.0 76.4 1.0
NC C:HEC501 2.0 79.3 1.0
NB C:HEC501 2.1 77.8 1.0
ND C:HEC501 2.1 76.5 1.0
NE2 C:HIS38 2.2 69.5 1.0
SD C:MET183 2.2 82.2 1.0
CE1 C:HIS38 3.0 67.3 1.0
C1A C:HEC501 3.0 74.0 1.0
C1C C:HEC501 3.0 75.8 1.0
C4C C:HEC501 3.0 73.2 1.0
C4D C:HEC501 3.0 74.6 1.0
C4B C:HEC501 3.1 72.9 1.0
C4A C:HEC501 3.1 72.4 1.0
C1D C:HEC501 3.1 73.2 1.0
C1B C:HEC501 3.1 75.0 1.0
CD2 C:HIS38 3.4 69.7 1.0
CHA C:HEC501 3.4 74.0 1.0
CHC C:HEC501 3.4 74.7 1.0
CE C:MET183 3.4 71.8 1.0
CHD C:HEC501 3.4 71.8 1.0
CHB C:HEC501 3.5 71.0 1.0
CG C:MET183 3.6 75.6 1.0
ND1 C:HIS38 4.2 64.8 1.0
CB C:MET183 4.2 78.6 1.0
C2A C:HEC501 4.2 74.5 1.0
C2C C:HEC501 4.2 72.4 1.0
C3C C:HEC501 4.2 74.4 1.0
C3A C:HEC501 4.3 69.8 1.0
C3B C:HEC501 4.3 71.4 1.0
C3D C:HEC501 4.3 72.0 1.0
C2B C:HEC501 4.3 71.0 1.0
C2D C:HEC501 4.3 73.5 1.0
CG C:HIS38 4.4 68.1 1.0

Iron binding site 6 out of 10 in 29yc

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Iron binding site 6 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:113.2
occ:1.00
 FE1 D:FES501 0.0 113.2 1.0
S1 D:FES501 2.2 102.2 1.0
S2 D:FES501 2.2 104.6 1.0
SG D:CYS153 2.3 93.0 1.0
SG D:CYS133 2.3 91.6 1.0
FE2 D:FES501 2.7 110.6 1.0
CB D:CYS133 3.2 77.4 1.0
CB D:CYS153 3.4 83.7 1.0
CB D:HIS135 3.9 85.0 1.0
CB D:CYS138 4.1 100.2 1.0
ND1 D:HIS135 4.3 89.3 1.0
CB D:CYS155 4.4 92.9 1.0
OG D:SER158 4.5 91.6 1.0
CG D:HIS135 4.6 85.8 1.0
N D:LEU136 4.6 85.4 1.0
N D:CYS138 4.6 93.3 1.0
ND1 D:HIS156 4.6 94.1 1.0
CA D:CYS133 4.7 74.4 1.0
CA D:CYS153 4.8 84.3 1.0
CB D:SER158 4.8 89.7 1.0
N D:HIS135 4.8 83.2 1.0
CA D:CYS138 4.8 88.9 1.0
SG D:CYS138 4.9 150.7 1.0
O D:CYS138 4.9 91.1 1.0
N D:HIS156 4.9 91.5 1.0
CA D:HIS135 4.9 80.3 1.0

Iron binding site 7 out of 10 in 29yc

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Iron binding site 7 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:110.6
occ:1.00
 FE2 D:FES501 0.0 110.6 1.0
ND1 D:HIS156 2.1 94.1 1.0
ND1 D:HIS135 2.1 89.3 1.0
S2 D:FES501 2.2 104.6 1.0
S1 D:FES501 2.2 102.2 1.0
FE1 D:FES501 2.7 113.2 1.0
CG D:HIS156 3.0 89.3 1.0
CE1 D:HIS135 3.1 84.4 1.0
CG D:HIS135 3.2 85.8 1.0
CE1 D:HIS156 3.2 93.0 1.0
CB D:HIS156 3.2 88.6 1.0
CB D:HIS135 3.5 85.0 1.0
N D:HIS156 3.7 91.5 1.0
CB D:CYS155 4.1 92.9 1.0
CA D:HIS156 4.1 88.4 1.0
CD2 D:HIS156 4.1 85.0 1.0
NE2 D:HIS156 4.2 89.2 1.0
NE2 D:HIS135 4.2 83.5 1.0
CD2 D:HIS135 4.3 85.1 1.0
SG D:CYS153 4.3 93.0 1.0
C D:CYS155 4.4 91.6 1.0
N D:LEU136 4.5 85.4 1.0
SG D:CYS133 4.5 91.6 1.0
CB D:LEU136 4.7 85.0 1.0
CA D:CYS155 4.8 89.2 1.0
OG D:SER158 4.8 91.6 1.0
CA D:HIS135 4.8 80.3 1.0
C D:HIS156 4.9 93.0 1.0
CG D:PRO170 4.9 81.7 1.0
C D:HIS135 4.9 85.5 1.0
CG D:LEU136 5.0 87.5 1.0

Iron binding site 8 out of 10 in 29yc

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Iron binding site 8 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe501

b:89.6
occ:1.00
 FE E:HEM501 0.0 89.6 1.0
ND E:HEM501 2.0 64.8 1.0
NC E:HEM501 2.0 67.9 1.0
NA E:HEM501 2.0 63.9 1.0
NB E:HEM501 2.0 63.9 1.0
NE2 E:HIS198 2.2 63.9 1.0
NE2 E:HIS97 2.2 64.8 1.0
CE1 E:HIS198 3.0 59.5 1.0
C4D E:HEM501 3.0 63.3 1.0
C4C E:HEM501 3.0 65.9 1.0
C1D E:HEM501 3.0 65.7 1.0
C1C E:HEM501 3.1 64.4 1.0
C4B E:HEM501 3.1 62.0 1.0
C1A E:HEM501 3.1 59.5 1.0
C1B E:HEM501 3.1 62.1 1.0
C4A E:HEM501 3.1 60.8 1.0
CE1 E:HIS97 3.1 62.2 1.0
CD2 E:HIS97 3.3 61.3 1.0
CD2 E:HIS198 3.3 62.5 1.0
CHC E:HEM501 3.4 61.1 1.0
CHD E:HEM501 3.4 66.5 1.0
CHA E:HEM501 3.4 60.3 1.0
CHB E:HEM501 3.4 57.8 1.0
ND1 E:HIS198 4.2 62.4 1.0
C3D E:HEM501 4.3 65.5 1.0
C2D E:HEM501 4.3 63.9 1.0
C3C E:HEM501 4.3 63.3 1.0
C2C E:HEM501 4.3 64.8 1.0
C3B E:HEM501 4.3 64.2 1.0
C2A E:HEM501 4.3 62.5 1.0
C3A E:HEM501 4.3 62.6 1.0
C2B E:HEM501 4.3 65.8 1.0
ND1 E:HIS97 4.3 62.9 1.0
CG E:HIS198 4.4 64.5 1.0
CG E:HIS97 4.4 63.3 1.0

Iron binding site 9 out of 10 in 29yc

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Iron binding site 9 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe502

b:90.5
occ:1.00
 FE E:HEM502 0.0 90.5 1.0
ND E:HEM502 2.0 72.3 1.0
NA E:HEM502 2.0 74.8 1.0
NB E:HEM502 2.0 72.0 1.0
NC E:HEM502 2.0 70.6 1.0
NE2 E:HIS212 2.3 67.3 1.0
NE2 E:HIS111 2.3 71.2 1.0
C4C E:HEM502 3.0 65.4 1.0
C4D E:HEM502 3.0 69.3 1.0
C1D E:HEM502 3.0 69.2 1.0
C4A E:HEM502 3.0 76.0 1.0
C1C E:HEM502 3.0 69.9 1.0
C1A E:HEM502 3.0 68.3 1.0
C1B E:HEM502 3.0 65.9 1.0
C4B E:HEM502 3.1 66.3 1.0
CD2 E:HIS111 3.1 68.8 1.0
CD2 E:HIS212 3.2 64.7 1.0
CE1 E:HIS212 3.3 69.5 1.0
CHD E:HEM502 3.4 65.3 1.0
CHB E:HEM502 3.4 67.4 1.0
CHA E:HEM502 3.4 68.6 1.0
CHC E:HEM502 3.4 63.4 1.0
CE1 E:HIS111 3.5 73.1 1.0
C3C E:HEM502 4.2 67.2 1.0
C2C E:HEM502 4.2 67.1 1.0
C3D E:HEM502 4.3 68.0 1.0
C2D E:HEM502 4.3 72.1 1.0
C3A E:HEM502 4.3 74.2 1.0
C2A E:HEM502 4.3 71.5 1.0
C2B E:HEM502 4.3 60.7 1.0
C3B E:HEM502 4.3 62.7 1.0
CG E:HIS111 4.3 69.9 1.0
ND1 E:HIS212 4.3 75.8 1.0
CG E:HIS212 4.4 71.5 1.0
ND1 E:HIS111 4.5 78.1 1.0

Iron binding site 10 out of 10 in 29yc

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Iron binding site 10 out of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position


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 Rhodobacter Capsulatus Cytochrome BC1 Dimer with Both Rieske Proteins in the C Position within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe501

b:93.8
occ:1.00
 FE F:HEC501 0.0 93.8 1.0
NA F:HEC501 2.0 75.2 1.0
NC F:HEC501 2.0 78.5 1.0
NB F:HEC501 2.1 77.0 1.0
ND F:HEC501 2.1 75.5 1.0
NE2 F:HIS38 2.2 68.3 1.0
SD F:MET183 2.2 79.8 1.0
CE1 F:HIS38 3.0 65.9 1.0
C1A F:HEC501 3.0 72.6 1.0
C1C F:HEC501 3.0 74.5 1.0
C4C F:HEC501 3.0 71.9 1.0
C4D F:HEC501 3.0 73.0 1.0
C4B F:HEC501 3.1 72.1 1.0
C4A F:HEC501 3.1 71.3 1.0
C1D F:HEC501 3.1 71.9 1.0
C1B F:HEC501 3.1 73.8 1.0
CD2 F:HIS38 3.4 68.5 1.0
CHA F:HEC501 3.4 72.4 1.0
CHC F:HEC501 3.4 73.4 1.0
CE F:MET183 3.4 70.2 1.0
CHD F:HEC501 3.4 70.5 1.0
CHB F:HEC501 3.5 69.5 1.0
CG F:MET183 3.6 74.0 1.0
ND1 F:HIS38 4.2 63.5 1.0
CB F:MET183 4.2 77.2 1.0
C2A F:HEC501 4.2 73.2 1.0
C2C F:HEC501 4.2 71.2 1.0
C3C F:HEC501 4.2 73.1 1.0
C3A F:HEC501 4.3 68.6 1.0
C3B F:HEC501 4.3 70.2 1.0
C3D F:HEC501 4.3 70.4 1.0
C2B F:HEC501 4.3 69.8 1.0
C2D F:HEC501 4.3 71.8 1.0
CG F:HIS38 4.4 67.0 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 09:43:37 2026

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