Iron in PDB 29yd: Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate Position
Enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate Position
All present enzymatic activity of Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position
(pdb code 29yd). 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 One Rieske Protein in the C Position and One in An Intermediate Position, PDB code: 29yd:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 10 in 29yd
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Iron Binding Sites List in 29yd
Iron binding site 1 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:137.5
occ:1.00
|
FE1
|
A:FES501
|
0.0
|
137.5
|
1.0
|
|
S1
|
A:FES501
|
2.2
|
108.3
|
1.0
|
|
S2
|
A:FES501
|
2.2
|
121.4
|
1.0
|
|
SG
|
A:CYS133
|
2.2
|
105.2
|
1.0
|
|
SG
|
A:CYS153
|
2.3
|
102.6
|
1.0
|
|
FE2
|
A:FES501
|
2.7
|
134.4
|
1.0
|
|
CB
|
A:CYS133
|
3.2
|
93.5
|
1.0
|
|
CB
|
A:CYS153
|
3.3
|
89.0
|
1.0
|
|
CB
|
A:HIS135
|
3.9
|
98.9
|
1.0
|
|
CB
|
A:CYS138
|
4.2
|
96.7
|
1.0
|
|
ND1
|
A:HIS135
|
4.3
|
102.9
|
1.0
|
|
OG
|
A:SER158
|
4.4
|
83.9
|
1.0
|
|
CB
|
A:CYS155
|
4.6
|
95.0
|
1.0
|
|
CG
|
A:HIS135
|
4.6
|
100.2
|
1.0
|
|
CA
|
A:CYS133
|
4.6
|
89.3
|
1.0
|
|
CB
|
A:SER158
|
4.6
|
87.7
|
1.0
|
|
N
|
A:LEU136
|
4.7
|
94.5
|
1.0
|
|
ND1
|
A:HIS156
|
4.7
|
116.2
|
1.0
|
|
CA
|
A:CYS153
|
4.7
|
89.9
|
1.0
|
|
N
|
A:CYS138
|
4.7
|
91.7
|
1.0
|
|
N
|
A:HIS135
|
4.8
|
95.1
|
1.0
|
|
CA
|
A:HIS135
|
4.9
|
96.8
|
1.0
|
|
N
|
A:HIS156
|
4.9
|
103.1
|
1.0
|
|
O
|
A:CYS138
|
4.9
|
93.4
|
1.0
|
|
CA
|
A:CYS138
|
5.0
|
89.6
|
1.0
|
|
SG
|
A:CYS138
|
5.0
|
112.8
|
1.0
|
|
Iron binding site 2 out
of 10 in 29yd
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Iron Binding Sites List in 29yd
Iron binding site 2 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:134.4
occ:1.00
|
FE2
|
A:FES501
|
0.0
|
134.4
|
1.0
|
|
ND1
|
A:HIS135
|
2.1
|
102.9
|
1.0
|
|
S1
|
A:FES501
|
2.2
|
108.3
|
1.0
|
|
S2
|
A:FES501
|
2.2
|
121.4
|
1.0
|
|
ND1
|
A:HIS156
|
2.3
|
116.2
|
1.0
|
|
FE1
|
A:FES501
|
2.7
|
137.5
|
1.0
|
|
CG
|
A:HIS156
|
3.1
|
113.2
|
1.0
|
|
CG
|
A:HIS135
|
3.1
|
100.2
|
1.0
|
|
CE1
|
A:HIS135
|
3.1
|
100.2
|
1.0
|
|
CB
|
A:HIS156
|
3.2
|
106.5
|
1.0
|
|
CE1
|
A:HIS156
|
3.3
|
111.8
|
1.0
|
|
CB
|
A:HIS135
|
3.4
|
98.9
|
1.0
|
|
N
|
A:HIS156
|
3.7
|
103.1
|
1.0
|
|
CA
|
A:HIS156
|
4.0
|
104.6
|
1.0
|
|
CB
|
A:CYS155
|
4.2
|
95.0
|
1.0
|
|
NE2
|
A:HIS135
|
4.2
|
94.3
|
1.0
|
|
CD2
|
A:HIS135
|
4.2
|
96.5
|
1.0
|
|
CD2
|
A:HIS156
|
4.2
|
112.0
|
1.0
|
|
SG
|
A:CYS153
|
4.2
|
102.6
|
1.0
|
|
NE2
|
A:HIS156
|
4.3
|
113.7
|
1.0
|
|
C
|
A:CYS155
|
4.4
|
103.6
|
1.0
|
|
SG
|
A:CYS133
|
4.4
|
105.2
|
1.0
|
|
N
|
A:LEU136
|
4.5
|
94.5
|
1.0
|
|
OG
|
A:SER158
|
4.6
|
83.9
|
1.0
|
|
CA
|
A:HIS135
|
4.7
|
96.8
|
1.0
|
|
CG
|
A:PRO170
|
4.8
|
82.9
|
1.0
|
|
C
|
A:HIS156
|
4.8
|
102.3
|
1.0
|
|
CA
|
A:CYS155
|
4.9
|
93.8
|
1.0
|
|
CB
|
A:LEU136
|
4.9
|
93.2
|
1.0
|
|
C
|
A:HIS135
|
4.9
|
95.5
|
1.0
|
|
Iron binding site 3 out
of 10 in 29yd
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Iron Binding Sites List in 29yd
Iron binding site 3 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe501
b:87.4
occ:1.00
|
FE
|
B:HEM501
|
0.0
|
87.4
|
1.0
|
|
ND
|
B:HEM501
|
2.0
|
66.7
|
1.0
|
|
NA
|
B:HEM501
|
2.0
|
60.5
|
1.0
|
|
NB
|
B:HEM501
|
2.0
|
69.0
|
1.0
|
|
NC
|
B:HEM501
|
2.0
|
66.7
|
1.0
|
|
NE2
|
B:HIS198
|
2.2
|
64.8
|
1.0
|
|
NE2
|
B:HIS97
|
2.2
|
63.1
|
1.0
|
|
CE1
|
B:HIS198
|
3.0
|
61.5
|
1.0
|
|
C4D
|
B:HEM501
|
3.0
|
63.6
|
1.0
|
|
C1A
|
B:HEM501
|
3.0
|
59.6
|
1.0
|
|
C1B
|
B:HEM501
|
3.0
|
62.2
|
1.0
|
|
C1D
|
B:HEM501
|
3.0
|
67.3
|
1.0
|
|
C4A
|
B:HEM501
|
3.0
|
56.6
|
1.0
|
|
C4B
|
B:HEM501
|
3.1
|
68.9
|
1.0
|
|
C1C
|
B:HEM501
|
3.1
|
60.4
|
1.0
|
|
C4C
|
B:HEM501
|
3.1
|
62.7
|
1.0
|
|
CE1
|
B:HIS97
|
3.1
|
60.0
|
1.0
|
|
CD2
|
B:HIS97
|
3.3
|
60.0
|
1.0
|
|
CD2
|
B:HIS198
|
3.3
|
62.2
|
1.0
|
|
CHA
|
B:HEM501
|
3.4
|
62.4
|
1.0
|
|
CHB
|
B:HEM501
|
3.4
|
52.8
|
1.0
|
|
CHC
|
B:HEM501
|
3.4
|
56.1
|
1.0
|
|
CHD
|
B:HEM501
|
3.4
|
67.0
|
1.0
|
|
ND1
|
B:HIS198
|
4.2
|
65.4
|
1.0
|
|
C3D
|
B:HEM501
|
4.3
|
66.8
|
1.0
|
|
C2D
|
B:HEM501
|
4.3
|
65.9
|
1.0
|
|
C3A
|
B:HEM501
|
4.3
|
55.9
|
1.0
|
|
C2A
|
B:HEM501
|
4.3
|
57.5
|
1.0
|
|
C2B
|
B:HEM501
|
4.3
|
62.0
|
1.0
|
|
C3B
|
B:HEM501
|
4.3
|
67.1
|
1.0
|
|
C2C
|
B:HEM501
|
4.3
|
61.1
|
1.0
|
|
C3C
|
B:HEM501
|
4.3
|
54.2
|
1.0
|
|
ND1
|
B:HIS97
|
4.3
|
60.8
|
1.0
|
|
CG
|
B:HIS198
|
4.4
|
65.5
|
1.0
|
|
CG
|
B:HIS97
|
4.4
|
60.8
|
1.0
|
|
Iron binding site 4 out
of 10 in 29yd
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Iron Binding Sites List in 29yd
Iron binding site 4 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe502
b:88.4
occ:1.00
|
FE
|
B:HEM502
|
0.0
|
88.4
|
1.0
|
|
ND
|
B:HEM502
|
2.0
|
66.0
|
1.0
|
|
NA
|
B:HEM502
|
2.0
|
72.1
|
1.0
|
|
NB
|
B:HEM502
|
2.0
|
73.2
|
1.0
|
|
NC
|
B:HEM502
|
2.0
|
75.4
|
1.0
|
|
NE2
|
B:HIS212
|
2.3
|
72.8
|
1.0
|
|
NE2
|
B:HIS111
|
2.3
|
74.2
|
1.0
|
|
C4D
|
B:HEM502
|
3.0
|
68.4
|
1.0
|
|
C1D
|
B:HEM502
|
3.0
|
71.3
|
1.0
|
|
C4C
|
B:HEM502
|
3.0
|
69.3
|
1.0
|
|
C1A
|
B:HEM502
|
3.0
|
65.8
|
1.0
|
|
C4A
|
B:HEM502
|
3.0
|
74.2
|
1.0
|
|
C1B
|
B:HEM502
|
3.0
|
60.5
|
1.0
|
|
C1C
|
B:HEM502
|
3.0
|
71.8
|
1.0
|
|
C4B
|
B:HEM502
|
3.0
|
72.6
|
1.0
|
|
CD2
|
B:HIS111
|
3.1
|
68.8
|
1.0
|
|
CD2
|
B:HIS212
|
3.2
|
73.6
|
1.0
|
|
CE1
|
B:HIS212
|
3.3
|
73.3
|
1.0
|
|
CHD
|
B:HEM502
|
3.4
|
71.0
|
1.0
|
|
CHA
|
B:HEM502
|
3.4
|
67.9
|
1.0
|
|
CHB
|
B:HEM502
|
3.4
|
61.9
|
1.0
|
|
CHC
|
B:HEM502
|
3.4
|
74.4
|
1.0
|
|
CE1
|
B:HIS111
|
3.5
|
79.8
|
1.0
|
|
C3C
|
B:HEM502
|
4.2
|
66.8
|
1.0
|
|
C2C
|
B:HEM502
|
4.2
|
67.7
|
1.0
|
|
C3D
|
B:HEM502
|
4.3
|
72.2
|
1.0
|
|
C2D
|
B:HEM502
|
4.3
|
71.2
|
1.0
|
|
C3A
|
B:HEM502
|
4.3
|
76.0
|
1.0
|
|
C2A
|
B:HEM502
|
4.3
|
71.3
|
1.0
|
|
C2B
|
B:HEM502
|
4.3
|
56.7
|
1.0
|
|
C3B
|
B:HEM502
|
4.3
|
60.5
|
1.0
|
|
CG
|
B:HIS111
|
4.3
|
73.6
|
1.0
|
|
ND1
|
B:HIS212
|
4.3
|
73.4
|
1.0
|
|
CG
|
B:HIS212
|
4.4
|
70.2
|
1.0
|
|
ND1
|
B:HIS111
|
4.5
|
80.6
|
1.0
|
|
Iron binding site 5 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 5 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:102.7
occ:1.00
|
FE
|
C:HEC501
|
0.0
|
102.7
|
1.0
|
|
NC
|
C:HEC501
|
2.0
|
82.8
|
1.0
|
|
NA
|
C:HEC501
|
2.0
|
75.3
|
1.0
|
|
NB
|
C:HEC501
|
2.1
|
75.8
|
1.0
|
|
ND
|
C:HEC501
|
2.1
|
77.4
|
1.0
|
|
NE2
|
C:HIS38
|
2.2
|
67.8
|
1.0
|
|
SD
|
C:MET183
|
2.2
|
87.0
|
1.0
|
|
CE1
|
C:HIS38
|
3.0
|
66.2
|
1.0
|
|
C1A
|
C:HEC501
|
3.0
|
75.3
|
1.0
|
|
C1C
|
C:HEC501
|
3.0
|
74.4
|
1.0
|
|
C4C
|
C:HEC501
|
3.0
|
78.5
|
1.0
|
|
C4D
|
C:HEC501
|
3.1
|
76.5
|
1.0
|
|
C4B
|
C:HEC501
|
3.1
|
76.0
|
1.0
|
|
C4A
|
C:HEC501
|
3.1
|
66.4
|
1.0
|
|
C1D
|
C:HEC501
|
3.1
|
74.2
|
1.0
|
|
C1B
|
C:HEC501
|
3.1
|
69.0
|
1.0
|
|
CD2
|
C:HIS38
|
3.3
|
71.0
|
1.0
|
|
CHA
|
C:HEC501
|
3.4
|
77.7
|
1.0
|
|
CHC
|
C:HEC501
|
3.4
|
76.4
|
1.0
|
|
CHD
|
C:HEC501
|
3.4
|
73.7
|
1.0
|
|
CE
|
C:MET183
|
3.4
|
81.2
|
1.0
|
|
CHB
|
C:HEC501
|
3.5
|
65.7
|
1.0
|
|
CG
|
C:MET183
|
3.6
|
81.5
|
1.0
|
|
ND1
|
C:HIS38
|
4.2
|
60.2
|
1.0
|
|
CB
|
C:MET183
|
4.2
|
82.5
|
1.0
|
|
C2C
|
C:HEC501
|
4.2
|
73.8
|
1.0
|
|
C2A
|
C:HEC501
|
4.2
|
73.0
|
1.0
|
|
C3C
|
C:HEC501
|
4.2
|
78.7
|
1.0
|
|
C3A
|
C:HEC501
|
4.3
|
67.2
|
1.0
|
|
C3B
|
C:HEC501
|
4.3
|
71.1
|
1.0
|
|
C2B
|
C:HEC501
|
4.3
|
68.9
|
1.0
|
|
C3D
|
C:HEC501
|
4.3
|
74.8
|
1.0
|
|
C2D
|
C:HEC501
|
4.3
|
76.3
|
1.0
|
|
CG
|
C:HIS38
|
4.4
|
66.8
|
1.0
|
|
Iron binding site 6 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 6 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:120.8
occ:1.00
|
FE1
|
D:FES501
|
0.0
|
120.8
|
1.0
|
|
S1
|
D:FES501
|
2.2
|
117.3
|
1.0
|
|
S2
|
D:FES501
|
2.2
|
119.0
|
1.0
|
|
SG
|
D:CYS153
|
2.3
|
105.5
|
1.0
|
|
SG
|
D:CYS133
|
2.3
|
100.2
|
1.0
|
|
FE2
|
D:FES501
|
2.7
|
114.7
|
1.0
|
|
CB
|
D:CYS133
|
3.2
|
91.0
|
1.0
|
|
CB
|
D:CYS153
|
3.4
|
94.7
|
1.0
|
|
CB
|
D:HIS135
|
3.9
|
97.5
|
1.0
|
|
CB
|
D:CYS138
|
4.0
|
105.8
|
1.0
|
|
ND1
|
D:HIS135
|
4.3
|
103.7
|
1.0
|
|
CB
|
D:CYS155
|
4.4
|
100.8
|
1.0
|
|
CG
|
D:HIS135
|
4.6
|
100.0
|
1.0
|
|
N
|
D:LEU136
|
4.6
|
100.6
|
1.0
|
|
OG
|
D:SER158
|
4.6
|
99.2
|
1.0
|
|
N
|
D:CYS138
|
4.6
|
100.2
|
1.0
|
|
ND1
|
D:HIS156
|
4.6
|
99.5
|
1.0
|
|
CA
|
D:CYS133
|
4.7
|
92.0
|
1.0
|
|
CA
|
D:CYS153
|
4.8
|
93.3
|
1.0
|
|
CA
|
D:CYS138
|
4.8
|
92.7
|
1.0
|
|
N
|
D:HIS135
|
4.8
|
98.2
|
1.0
|
|
SG
|
D:CYS138
|
4.8
|
127.1
|
1.0
|
|
CB
|
D:SER158
|
4.8
|
98.0
|
1.0
|
|
O
|
D:CYS138
|
4.8
|
100.6
|
1.0
|
|
CA
|
D:HIS135
|
4.9
|
94.9
|
1.0
|
|
N
|
D:HIS156
|
4.9
|
100.5
|
1.0
|
|
Iron binding site 7 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 7 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:114.7
occ:1.00
|
FE2
|
D:FES501
|
0.0
|
114.7
|
1.0
|
|
ND1
|
D:HIS156
|
2.1
|
99.5
|
1.0
|
|
ND1
|
D:HIS135
|
2.2
|
103.7
|
1.0
|
|
S1
|
D:FES501
|
2.2
|
117.3
|
1.0
|
|
S2
|
D:FES501
|
2.2
|
119.0
|
1.0
|
|
FE1
|
D:FES501
|
2.7
|
120.8
|
1.0
|
|
CG
|
D:HIS156
|
3.0
|
99.9
|
1.0
|
|
CE1
|
D:HIS135
|
3.1
|
96.0
|
1.0
|
|
CE1
|
D:HIS156
|
3.1
|
104.5
|
1.0
|
|
CG
|
D:HIS135
|
3.2
|
100.0
|
1.0
|
|
CB
|
D:HIS156
|
3.3
|
99.6
|
1.0
|
|
CB
|
D:HIS135
|
3.5
|
97.5
|
1.0
|
|
N
|
D:HIS156
|
3.7
|
100.5
|
1.0
|
|
CB
|
D:CYS155
|
4.0
|
100.8
|
1.0
|
|
CA
|
D:HIS156
|
4.1
|
98.1
|
1.0
|
|
CD2
|
D:HIS156
|
4.1
|
100.9
|
1.0
|
|
NE2
|
D:HIS156
|
4.2
|
104.2
|
1.0
|
|
NE2
|
D:HIS135
|
4.2
|
93.3
|
1.0
|
|
CD2
|
D:HIS135
|
4.3
|
97.0
|
1.0
|
|
SG
|
D:CYS153
|
4.3
|
105.5
|
1.0
|
|
C
|
D:CYS155
|
4.3
|
99.2
|
1.0
|
|
N
|
D:LEU136
|
4.5
|
100.6
|
1.0
|
|
SG
|
D:CYS133
|
4.5
|
100.2
|
1.0
|
|
CB
|
D:LEU136
|
4.7
|
95.9
|
1.0
|
|
CA
|
D:CYS155
|
4.8
|
100.4
|
1.0
|
|
CA
|
D:HIS135
|
4.8
|
94.9
|
1.0
|
|
OG
|
D:SER158
|
4.8
|
99.2
|
1.0
|
|
C
|
D:HIS156
|
4.9
|
99.0
|
1.0
|
|
C
|
D:HIS135
|
4.9
|
99.2
|
1.0
|
|
CG
|
D:PRO170
|
4.9
|
92.9
|
1.0
|
|
CG
|
D:LEU136
|
4.9
|
102.2
|
1.0
|
|
CD1
|
D:LEU136
|
5.0
|
100.9
|
1.0
|
|
Iron binding site 8 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 8 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe501
b:89.0
occ:1.00
|
FE
|
E:HEM501
|
0.0
|
89.0
|
1.0
|
|
ND
|
E:HEM501
|
2.0
|
63.7
|
1.0
|
|
NA
|
E:HEM501
|
2.0
|
63.8
|
1.0
|
|
NC
|
E:HEM501
|
2.0
|
65.3
|
1.0
|
|
NB
|
E:HEM501
|
2.0
|
61.6
|
1.0
|
|
NE2
|
E:HIS198
|
2.2
|
66.1
|
1.0
|
|
NE2
|
E:HIS97
|
2.2
|
66.7
|
1.0
|
|
CE1
|
E:HIS198
|
3.0
|
59.0
|
1.0
|
|
C4D
|
E:HEM501
|
3.0
|
62.9
|
1.0
|
|
C1D
|
E:HEM501
|
3.0
|
65.7
|
1.0
|
|
C1A
|
E:HEM501
|
3.0
|
58.7
|
1.0
|
|
C4C
|
E:HEM501
|
3.0
|
60.9
|
1.0
|
|
C4A
|
E:HEM501
|
3.0
|
61.4
|
1.0
|
|
C1B
|
E:HEM501
|
3.1
|
61.6
|
1.0
|
|
C1C
|
E:HEM501
|
3.1
|
63.9
|
1.0
|
|
C4B
|
E:HEM501
|
3.1
|
58.9
|
1.0
|
|
CE1
|
E:HIS97
|
3.1
|
65.6
|
1.0
|
|
CD2
|
E:HIS97
|
3.3
|
67.6
|
1.0
|
|
CD2
|
E:HIS198
|
3.3
|
67.2
|
1.0
|
|
CHA
|
E:HEM501
|
3.4
|
60.8
|
1.0
|
|
CHD
|
E:HEM501
|
3.4
|
63.7
|
1.0
|
|
CHB
|
E:HEM501
|
3.4
|
64.3
|
1.0
|
|
CHC
|
E:HEM501
|
3.4
|
57.2
|
1.0
|
|
ND1
|
E:HIS198
|
4.2
|
61.7
|
1.0
|
|
C3D
|
E:HEM501
|
4.3
|
63.5
|
1.0
|
|
C2D
|
E:HEM501
|
4.3
|
66.2
|
1.0
|
|
C3A
|
E:HEM501
|
4.3
|
60.0
|
1.0
|
|
C2A
|
E:HEM501
|
4.3
|
62.8
|
1.0
|
|
C2B
|
E:HEM501
|
4.3
|
58.9
|
1.0
|
|
C2C
|
E:HEM501
|
4.3
|
62.1
|
1.0
|
|
C3C
|
E:HEM501
|
4.3
|
56.0
|
1.0
|
|
C3B
|
E:HEM501
|
4.3
|
60.6
|
1.0
|
|
ND1
|
E:HIS97
|
4.3
|
66.7
|
1.0
|
|
CG
|
E:HIS198
|
4.4
|
65.6
|
1.0
|
|
CG
|
E:HIS97
|
4.4
|
68.7
|
1.0
|
|
Iron binding site 9 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 9 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe502
b:89.5
occ:1.00
|
FE
|
E:HEM502
|
0.0
|
89.5
|
1.0
|
|
ND
|
E:HEM502
|
2.0
|
72.8
|
1.0
|
|
NA
|
E:HEM502
|
2.0
|
74.3
|
1.0
|
|
NB
|
E:HEM502
|
2.0
|
71.5
|
1.0
|
|
NC
|
E:HEM502
|
2.0
|
70.7
|
1.0
|
|
NE2
|
E:HIS212
|
2.3
|
69.1
|
1.0
|
|
NE2
|
E:HIS111
|
2.3
|
69.5
|
1.0
|
|
C1D
|
E:HEM502
|
3.0
|
71.7
|
1.0
|
|
C4C
|
E:HEM502
|
3.0
|
63.3
|
1.0
|
|
C4D
|
E:HEM502
|
3.0
|
69.8
|
1.0
|
|
C1C
|
E:HEM502
|
3.0
|
70.4
|
1.0
|
|
C4A
|
E:HEM502
|
3.0
|
74.5
|
1.0
|
|
C1B
|
E:HEM502
|
3.0
|
64.3
|
1.0
|
|
C1A
|
E:HEM502
|
3.0
|
68.3
|
1.0
|
|
C4B
|
E:HEM502
|
3.1
|
69.1
|
1.0
|
|
CD2
|
E:HIS111
|
3.1
|
67.2
|
1.0
|
|
CD2
|
E:HIS212
|
3.2
|
65.6
|
1.0
|
|
CE1
|
E:HIS212
|
3.3
|
73.4
|
1.0
|
|
CHD
|
E:HEM502
|
3.4
|
68.5
|
1.0
|
|
CHB
|
E:HEM502
|
3.4
|
65.3
|
1.0
|
|
CHA
|
E:HEM502
|
3.4
|
69.8
|
1.0
|
|
CHC
|
E:HEM502
|
3.4
|
69.2
|
1.0
|
|
CE1
|
E:HIS111
|
3.5
|
74.6
|
1.0
|
|
C2C
|
E:HEM502
|
4.2
|
65.9
|
1.0
|
|
C3C
|
E:HEM502
|
4.2
|
65.0
|
1.0
|
|
C2D
|
E:HEM502
|
4.3
|
71.5
|
1.0
|
|
C3D
|
E:HEM502
|
4.3
|
69.0
|
1.0
|
|
C3A
|
E:HEM502
|
4.3
|
73.4
|
1.0
|
|
C2A
|
E:HEM502
|
4.3
|
69.9
|
1.0
|
|
C2B
|
E:HEM502
|
4.3
|
61.1
|
1.0
|
|
C3B
|
E:HEM502
|
4.3
|
59.6
|
1.0
|
|
CG
|
E:HIS111
|
4.3
|
68.7
|
1.0
|
|
ND1
|
E:HIS212
|
4.3
|
77.1
|
1.0
|
|
CG
|
E:HIS212
|
4.4
|
72.0
|
1.0
|
|
ND1
|
E:HIS111
|
4.5
|
77.8
|
1.0
|
|
Iron binding site 10 out
of 10 in 29yd
Go back to
Iron Binding Sites List in 29yd
Iron binding site 10 out
of 10 in the Cryo-Em Structure of Rhodobacter Capsulatus Cytochrome BC1 Dimer with One Rieske Protein in the C Position and One in An Intermediate 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 One Rieske Protein in the C Position and One in An Intermediate Position within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Fe501
b:103.7
occ:1.00
|
FE
|
F:HEC501
|
0.0
|
103.7
|
1.0
|
|
NA
|
F:HEC501
|
2.0
|
71.1
|
1.0
|
|
NC
|
F:HEC501
|
2.0
|
80.3
|
1.0
|
|
ND
|
F:HEC501
|
2.1
|
76.6
|
1.0
|
|
NB
|
F:HEC501
|
2.1
|
75.9
|
1.0
|
|
NE2
|
F:HIS38
|
2.2
|
70.9
|
1.0
|
|
SD
|
F:MET183
|
2.2
|
76.8
|
1.0
|
|
CE1
|
F:HIS38
|
3.0
|
66.4
|
1.0
|
|
C1A
|
F:HEC501
|
3.0
|
70.0
|
1.0
|
|
C1C
|
F:HEC501
|
3.0
|
76.8
|
1.0
|
|
C4D
|
F:HEC501
|
3.0
|
71.7
|
1.0
|
|
C4C
|
F:HEC501
|
3.0
|
72.1
|
1.0
|
|
C4B
|
F:HEC501
|
3.1
|
70.8
|
1.0
|
|
C4A
|
F:HEC501
|
3.1
|
65.9
|
1.0
|
|
C1D
|
F:HEC501
|
3.1
|
75.7
|
1.0
|
|
C1B
|
F:HEC501
|
3.1
|
70.6
|
1.0
|
|
CD2
|
F:HIS38
|
3.4
|
74.2
|
1.0
|
|
CHA
|
F:HEC501
|
3.4
|
71.8
|
1.0
|
|
CHC
|
F:HEC501
|
3.4
|
76.3
|
1.0
|
|
CE
|
F:MET183
|
3.4
|
78.7
|
1.0
|
|
CHD
|
F:HEC501
|
3.4
|
70.8
|
1.0
|
|
CHB
|
F:HEC501
|
3.5
|
66.3
|
1.0
|
|
CG
|
F:MET183
|
3.6
|
83.1
|
1.0
|
|
ND1
|
F:HIS38
|
4.2
|
64.6
|
1.0
|
|
CB
|
F:MET183
|
4.2
|
81.2
|
1.0
|
|
C2A
|
F:HEC501
|
4.2
|
71.2
|
1.0
|
|
C2C
|
F:HEC501
|
4.2
|
77.6
|
1.0
|
|
C3C
|
F:HEC501
|
4.2
|
78.1
|
1.0
|
|
C3A
|
F:HEC501
|
4.3
|
63.6
|
1.0
|
|
C3D
|
F:HEC501
|
4.3
|
67.1
|
1.0
|
|
C3B
|
F:HEC501
|
4.3
|
67.6
|
1.0
|
|
C2B
|
F:HEC501
|
4.3
|
66.5
|
1.0
|
|
C2D
|
F:HEC501
|
4.3
|
75.5
|
1.0
|
|
CG
|
F:HIS38
|
4.4
|
70.3
|
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 09:43:24 2026
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