Iron in PDB 1zrt: Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
Enzymatic activity of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
All present enzymatic activity of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound:
1.10.2.2;
Protein crystallography data
The structure of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound, PDB code: 1zrt
was solved by
E.A.Berry,
L.S.Huang,
L.K.Saechao,
N.G.Pon,
M.Valkova-Valchanov,
F.Daldal,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
59.39 /
3.50
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
95.633,
154.360,
103.057,
90.00,
113.57,
90.00
|
|
R / Rfree (%)
|
30 /
35.8
|
Iron Binding Sites:
The binding sites of Iron atom in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
(pdb code 1zrt). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 10 binding sites of Iron where determined in the
Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound, PDB code: 1zrt:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 1 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:59.2
occ:1.00
|
FE
|
C:HEM501
|
0.0
|
59.2
|
1.0
|
|
NC
|
C:HEM501
|
1.8
|
3.5
|
1.0
|
|
NB
|
C:HEM501
|
1.8
|
3.5
|
1.0
|
|
NA
|
C:HEM501
|
1.8
|
3.5
|
1.0
|
|
ND
|
C:HEM501
|
1.9
|
3.5
|
1.0
|
|
NE2
|
C:HIS198
|
2.0
|
41.0
|
1.0
|
|
NE2
|
C:HIS97
|
2.0
|
46.5
|
1.0
|
|
CE1
|
C:HIS97
|
2.8
|
84.7
|
1.0
|
|
C4A
|
C:HEM501
|
2.9
|
3.5
|
1.0
|
|
C4C
|
C:HEM501
|
2.9
|
3.5
|
1.0
|
|
C1B
|
C:HEM501
|
2.9
|
23.5
|
1.0
|
|
C1C
|
C:HEM501
|
2.9
|
3.5
|
1.0
|
|
CE1
|
C:HIS198
|
2.9
|
54.2
|
1.0
|
|
C4B
|
C:HEM501
|
2.9
|
3.5
|
1.0
|
|
C1A
|
C:HEM501
|
3.0
|
14.2
|
1.0
|
|
C1D
|
C:HEM501
|
3.0
|
12.8
|
1.0
|
|
C4D
|
C:HEM501
|
3.0
|
3.5
|
1.0
|
|
CD2
|
C:HIS198
|
3.1
|
40.2
|
1.0
|
|
CD2
|
C:HIS97
|
3.1
|
79.5
|
1.0
|
|
CHB
|
C:HEM501
|
3.3
|
3.5
|
1.0
|
|
CHD
|
C:HEM501
|
3.3
|
3.5
|
1.0
|
|
CHC
|
C:HEM501
|
3.3
|
3.5
|
1.0
|
|
CHA
|
C:HEM501
|
3.4
|
3.5
|
1.0
|
|
ND1
|
C:HIS97
|
4.0
|
92.4
|
1.0
|
|
ND1
|
C:HIS198
|
4.1
|
46.1
|
1.0
|
|
C3C
|
C:HEM501
|
4.1
|
17.2
|
1.0
|
|
CG
|
C:HIS97
|
4.2
|
85.4
|
1.0
|
|
CG
|
C:HIS198
|
4.2
|
73.3
|
1.0
|
|
C2B
|
C:HEM501
|
4.2
|
9.7
|
1.0
|
|
C2C
|
C:HEM501
|
4.2
|
3.5
|
1.0
|
|
C3A
|
C:HEM501
|
4.2
|
38.7
|
1.0
|
|
C3B
|
C:HEM501
|
4.2
|
6.0
|
1.0
|
|
C2A
|
C:HEM501
|
4.3
|
25.3
|
1.0
|
|
C3D
|
C:HEM501
|
4.3
|
3.5
|
1.0
|
|
C2D
|
C:HEM501
|
4.4
|
13.6
|
1.0
|
|
CA
|
C:GLY146
|
4.8
|
40.6
|
1.0
|
|
Iron binding site 2 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 2 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe502
b:70.7
occ:1.00
|
FE
|
C:HEM502
|
0.0
|
70.7
|
1.0
|
|
NC
|
C:HEM502
|
1.9
|
14.6
|
1.0
|
|
NB
|
C:HEM502
|
1.9
|
32.4
|
1.0
|
|
ND
|
C:HEM502
|
1.9
|
35.0
|
1.0
|
|
NA
|
C:HEM502
|
1.9
|
30.2
|
1.0
|
|
NE2
|
C:HIS212
|
2.0
|
40.8
|
1.0
|
|
NE2
|
C:HIS111
|
2.0
|
48.9
|
1.0
|
|
CE1
|
C:HIS111
|
2.7
|
84.4
|
1.0
|
|
C1C
|
C:HEM502
|
2.9
|
39.5
|
1.0
|
|
C4D
|
C:HEM502
|
2.9
|
70.1
|
1.0
|
|
C1A
|
C:HEM502
|
2.9
|
69.3
|
1.0
|
|
C4B
|
C:HEM502
|
2.9
|
48.2
|
1.0
|
|
CD2
|
C:HIS212
|
3.0
|
30.8
|
1.0
|
|
C4C
|
C:HEM502
|
3.0
|
30.1
|
1.0
|
|
C1D
|
C:HEM502
|
3.0
|
46.4
|
1.0
|
|
C1B
|
C:HEM502
|
3.0
|
52.6
|
1.0
|
|
C4A
|
C:HEM502
|
3.0
|
51.6
|
1.0
|
|
CE1
|
C:HIS212
|
3.0
|
32.7
|
1.0
|
|
CD2
|
C:HIS111
|
3.1
|
61.9
|
1.0
|
|
CHA
|
C:HEM502
|
3.3
|
70.3
|
1.0
|
|
CHC
|
C:HEM502
|
3.3
|
36.5
|
1.0
|
|
CHD
|
C:HEM502
|
3.4
|
32.2
|
1.0
|
|
CHB
|
C:HEM502
|
3.4
|
54.7
|
1.0
|
|
ND1
|
C:HIS111
|
3.9
|
83.5
|
1.0
|
|
CG
|
C:HIS111
|
4.1
|
67.7
|
1.0
|
|
ND1
|
C:HIS212
|
4.1
|
71.0
|
1.0
|
|
CG
|
C:HIS212
|
4.1
|
63.0
|
1.0
|
|
C3D
|
C:HEM502
|
4.1
|
0.1
|
1.0
|
|
C2C
|
C:HEM502
|
4.1
|
55.5
|
1.0
|
|
C2D
|
C:HEM502
|
4.2
|
84.7
|
1.0
|
|
C2A
|
C:HEM502
|
4.2
|
85.0
|
1.0
|
|
C3C
|
C:HEM502
|
4.2
|
55.0
|
1.0
|
|
C3B
|
C:HEM502
|
4.2
|
57.7
|
1.0
|
|
C3A
|
C:HEM502
|
4.2
|
77.7
|
1.0
|
|
C2B
|
C:HEM502
|
4.3
|
59.3
|
1.0
|
|
O1A
|
C:HEM502
|
4.4
|
0.4
|
1.0
|
|
CA
|
C:GLY48
|
4.6
|
0.3
|
1.0
|
|
Iron binding site 3 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 3 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe501
b:0.8
occ:1.00
|
FE
|
D:HEC501
|
0.0
|
0.8
|
1.0
|
|
NA
|
D:HEC501
|
1.9
|
94.6
|
1.0
|
|
NC
|
D:HEC501
|
1.9
|
0.6
|
1.0
|
|
NB
|
D:HEC501
|
2.0
|
95.9
|
1.0
|
|
ND
|
D:HEC501
|
2.0
|
95.7
|
1.0
|
|
NE2
|
D:HIS38
|
2.0
|
0.1
|
1.0
|
|
SD
|
D:MET183
|
2.1
|
0.5
|
1.0
|
|
C4A
|
D:HEC501
|
2.9
|
0.0
|
1.0
|
|
C1A
|
D:HEC501
|
2.9
|
89.1
|
1.0
|
|
CD2
|
D:HIS38
|
2.9
|
0.9
|
1.0
|
|
C1C
|
D:HEC501
|
3.0
|
0.1
|
1.0
|
|
C1B
|
D:HEC501
|
3.0
|
93.8
|
1.0
|
|
CE1
|
D:HIS38
|
3.0
|
0.3
|
1.0
|
|
C4C
|
D:HEC501
|
3.0
|
0.2
|
1.0
|
|
C4B
|
D:HEC501
|
3.0
|
0.3
|
1.0
|
|
C1D
|
D:HEC501
|
3.0
|
96.6
|
1.0
|
|
C4D
|
D:HEC501
|
3.0
|
99.6
|
1.0
|
|
CHB
|
D:HEC501
|
3.3
|
92.2
|
1.0
|
|
CE
|
D:MET183
|
3.3
|
0.8
|
1.0
|
|
CHA
|
D:HEC501
|
3.4
|
84.6
|
1.0
|
|
CHC
|
D:HEC501
|
3.4
|
0.7
|
1.0
|
|
CHD
|
D:HEC501
|
3.4
|
0.6
|
1.0
|
|
CG
|
D:MET183
|
3.5
|
0.6
|
1.0
|
|
ND1
|
D:HIS38
|
4.1
|
0.2
|
1.0
|
|
CG
|
D:HIS38
|
4.1
|
0.5
|
1.0
|
|
C3A
|
D:HEC501
|
4.1
|
0.6
|
1.0
|
|
C2A
|
D:HEC501
|
4.1
|
0.3
|
1.0
|
|
C2C
|
D:HEC501
|
4.2
|
0.8
|
1.0
|
|
C3C
|
D:HEC501
|
4.2
|
0.6
|
1.0
|
|
C2D
|
D:HEC501
|
4.2
|
0.5
|
1.0
|
|
C3B
|
D:HEC501
|
4.2
|
0.2
|
1.0
|
|
C2B
|
D:HEC501
|
4.3
|
92.5
|
1.0
|
|
C3D
|
D:HEC501
|
4.3
|
0.2
|
1.0
|
|
CB
|
D:MET183
|
4.3
|
0.9
|
1.0
|
|
Iron binding site 4 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 4 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe501
b:85.5
occ:1.00
|
FE1
|
E:FES501
|
0.0
|
85.5
|
1.0
|
|
S2
|
E:FES501
|
2.2
|
50.3
|
1.0
|
|
S1
|
E:FES501
|
2.2
|
70.1
|
1.0
|
|
SG
|
E:CYS133
|
2.3
|
61.5
|
1.0
|
|
SG
|
E:CYS153
|
2.3
|
64.0
|
1.0
|
|
FE2
|
E:FES501
|
2.6
|
98.6
|
1.0
|
|
CB
|
E:CYS153
|
3.1
|
66.8
|
1.0
|
|
CB
|
E:CYS133
|
3.1
|
95.2
|
1.0
|
|
OG
|
E:SER158
|
3.2
|
0.0
|
1.0
|
|
CB
|
E:HIS135
|
4.0
|
78.4
|
1.0
|
|
CB
|
E:CYS155
|
4.1
|
0.1
|
1.0
|
|
ND1
|
E:HIS135
|
4.3
|
77.1
|
1.0
|
|
N
|
E:HIS156
|
4.4
|
59.5
|
1.0
|
|
ND1
|
E:HIS156
|
4.4
|
77.0
|
1.0
|
|
CB
|
E:SER158
|
4.5
|
0.8
|
1.0
|
|
CB
|
E:CYS138
|
4.5
|
90.1
|
1.0
|
|
CA
|
E:CYS153
|
4.5
|
70.4
|
1.0
|
|
N
|
E:LEU136
|
4.5
|
63.6
|
1.0
|
|
CA
|
E:CYS133
|
4.6
|
78.0
|
1.0
|
|
CG
|
E:HIS135
|
4.6
|
83.5
|
1.0
|
|
N
|
E:HIS135
|
4.8
|
64.8
|
1.0
|
|
N
|
E:CYS138
|
4.8
|
82.4
|
1.0
|
|
CA
|
E:HIS135
|
4.8
|
61.5
|
1.0
|
|
CA
|
E:CYS155
|
4.9
|
83.1
|
1.0
|
|
SG
|
E:CYS138
|
4.9
|
0.6
|
1.0
|
|
N
|
E:CYS155
|
4.9
|
80.8
|
1.0
|
|
C
|
E:CYS153
|
4.9
|
73.2
|
1.0
|
|
Iron binding site 5 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 5 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Fe501
b:98.6
occ:1.00
|
FE2
|
E:FES501
|
0.0
|
98.6
|
1.0
|
|
ND1
|
E:HIS156
|
2.1
|
77.0
|
1.0
|
|
ND1
|
E:HIS135
|
2.1
|
77.1
|
1.0
|
|
S2
|
E:FES501
|
2.2
|
50.3
|
1.0
|
|
S1
|
E:FES501
|
2.2
|
70.1
|
1.0
|
|
FE1
|
E:FES501
|
2.6
|
85.5
|
1.0
|
|
CG
|
E:HIS156
|
3.0
|
75.8
|
1.0
|
|
CG
|
E:HIS135
|
3.0
|
83.5
|
1.0
|
|
CE1
|
E:HIS135
|
3.1
|
94.9
|
1.0
|
|
CE1
|
E:HIS156
|
3.1
|
94.4
|
1.0
|
|
CB
|
E:HIS156
|
3.3
|
49.8
|
1.0
|
|
CB
|
E:HIS135
|
3.3
|
78.4
|
1.0
|
|
N
|
E:HIS156
|
3.7
|
59.5
|
1.0
|
|
CB
|
E:CYS155
|
3.9
|
0.1
|
1.0
|
|
N
|
E:LEU136
|
4.0
|
63.6
|
1.0
|
|
CB
|
E:LEU136
|
4.1
|
86.2
|
1.0
|
|
CA
|
E:HIS156
|
4.1
|
62.0
|
1.0
|
|
CD2
|
E:HIS135
|
4.1
|
81.3
|
1.0
|
|
CD2
|
E:HIS156
|
4.2
|
52.5
|
1.0
|
|
NE2
|
E:HIS135
|
4.2
|
69.5
|
1.0
|
|
NE2
|
E:HIS156
|
4.2
|
52.2
|
1.0
|
|
C
|
E:CYS155
|
4.3
|
81.0
|
1.0
|
|
SG
|
E:CYS153
|
4.3
|
64.0
|
1.0
|
|
SG
|
E:CYS133
|
4.4
|
61.5
|
1.0
|
|
C
|
E:HIS135
|
4.4
|
54.3
|
1.0
|
|
CA
|
E:HIS135
|
4.5
|
61.5
|
1.0
|
|
CA
|
E:LEU136
|
4.7
|
88.7
|
1.0
|
|
CA
|
E:CYS155
|
4.7
|
83.1
|
1.0
|
|
CG
|
E:LEU136
|
4.7
|
64.5
|
1.0
|
|
OG
|
E:SER158
|
4.8
|
0.0
|
1.0
|
|
CD1
|
E:LEU136
|
4.9
|
78.6
|
1.0
|
|
Iron binding site 6 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 6 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Fe501
b:46.3
occ:1.00
|
FE
|
P:HEM501
|
0.0
|
46.3
|
1.0
|
|
NB
|
P:HEM501
|
1.8
|
27.3
|
1.0
|
|
NA
|
P:HEM501
|
1.8
|
13.4
|
1.0
|
|
NC
|
P:HEM501
|
1.9
|
3.5
|
1.0
|
|
NE2
|
P:HIS97
|
2.0
|
35.5
|
1.0
|
|
NE2
|
P:HIS198
|
2.0
|
28.2
|
1.0
|
|
ND
|
P:HEM501
|
2.0
|
23.8
|
1.0
|
|
C4A
|
P:HEM501
|
2.8
|
14.5
|
1.0
|
|
CE1
|
P:HIS97
|
2.8
|
51.0
|
1.0
|
|
C1B
|
P:HEM501
|
2.9
|
28.9
|
1.0
|
|
C1C
|
P:HEM501
|
2.9
|
14.7
|
1.0
|
|
CE1
|
P:HIS198
|
2.9
|
57.5
|
1.0
|
|
C4B
|
P:HEM501
|
2.9
|
17.0
|
1.0
|
|
C4C
|
P:HEM501
|
3.0
|
25.0
|
1.0
|
|
C1A
|
P:HEM501
|
3.0
|
46.1
|
1.0
|
|
CD2
|
P:HIS198
|
3.1
|
43.6
|
1.0
|
|
C4D
|
P:HEM501
|
3.1
|
3.5
|
1.0
|
|
CD2
|
P:HIS97
|
3.1
|
69.2
|
1.0
|
|
C1D
|
P:HEM501
|
3.1
|
10.5
|
1.0
|
|
CHB
|
P:HEM501
|
3.2
|
14.2
|
1.0
|
|
CHC
|
P:HEM501
|
3.3
|
6.9
|
1.0
|
|
CHD
|
P:HEM501
|
3.4
|
4.1
|
1.0
|
|
CHA
|
P:HEM501
|
3.4
|
17.8
|
1.0
|
|
ND1
|
P:HIS97
|
4.0
|
92.4
|
1.0
|
|
ND1
|
P:HIS198
|
4.1
|
43.5
|
1.0
|
|
C2B
|
P:HEM501
|
4.1
|
22.4
|
1.0
|
|
C3A
|
P:HEM501
|
4.1
|
51.4
|
1.0
|
|
CG
|
P:HIS97
|
4.2
|
98.9
|
1.0
|
|
CG
|
P:HIS198
|
4.2
|
65.5
|
1.0
|
|
C3C
|
P:HEM501
|
4.2
|
5.8
|
1.0
|
|
C3B
|
P:HEM501
|
4.2
|
8.7
|
1.0
|
|
C2C
|
P:HEM501
|
4.2
|
12.8
|
1.0
|
|
C2A
|
P:HEM501
|
4.2
|
28.7
|
1.0
|
|
C3D
|
P:HEM501
|
4.4
|
35.2
|
1.0
|
|
C2D
|
P:HEM501
|
4.4
|
18.0
|
1.0
|
|
CA
|
P:GLY146
|
4.8
|
32.7
|
1.0
|
|
Iron binding site 7 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 7 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
P:Fe502
b:94.6
occ:1.00
|
FE
|
P:HEM502
|
0.0
|
94.6
|
1.0
|
|
ND
|
P:HEM502
|
1.9
|
56.4
|
1.0
|
|
NC
|
P:HEM502
|
1.9
|
49.6
|
1.0
|
|
NA
|
P:HEM502
|
1.9
|
11.3
|
1.0
|
|
NB
|
P:HEM502
|
1.9
|
57.5
|
1.0
|
|
NE2
|
P:HIS111
|
2.0
|
45.8
|
1.0
|
|
NE2
|
P:HIS212
|
2.0
|
50.0
|
1.0
|
|
CE1
|
P:HIS111
|
2.7
|
70.7
|
1.0
|
|
C1C
|
P:HEM502
|
2.9
|
83.6
|
1.0
|
|
C4D
|
P:HEM502
|
2.9
|
87.2
|
1.0
|
|
C1A
|
P:HEM502
|
2.9
|
77.2
|
1.0
|
|
C1D
|
P:HEM502
|
3.0
|
61.5
|
1.0
|
|
C4C
|
P:HEM502
|
3.0
|
60.9
|
1.0
|
|
C4B
|
P:HEM502
|
3.0
|
66.1
|
1.0
|
|
CE1
|
P:HIS212
|
3.0
|
34.9
|
1.0
|
|
CD2
|
P:HIS212
|
3.0
|
63.3
|
1.0
|
|
C4A
|
P:HEM502
|
3.0
|
58.6
|
1.0
|
|
C1B
|
P:HEM502
|
3.0
|
86.1
|
1.0
|
|
CD2
|
P:HIS111
|
3.1
|
85.2
|
1.0
|
|
CHA
|
P:HEM502
|
3.2
|
82.4
|
1.0
|
|
CHC
|
P:HEM502
|
3.3
|
73.3
|
1.0
|
|
CHD
|
P:HEM502
|
3.3
|
55.8
|
1.0
|
|
CHB
|
P:HEM502
|
3.4
|
70.4
|
1.0
|
|
ND1
|
P:HIS111
|
3.9
|
0.5
|
1.0
|
|
CG
|
P:HIS111
|
4.1
|
93.2
|
1.0
|
|
ND1
|
P:HIS212
|
4.1
|
76.8
|
1.0
|
|
C3D
|
P:HEM502
|
4.1
|
86.6
|
1.0
|
|
CG
|
P:HIS212
|
4.1
|
73.4
|
1.0
|
|
C2C
|
P:HEM502
|
4.1
|
77.4
|
1.0
|
|
C2D
|
P:HEM502
|
4.1
|
70.3
|
1.0
|
|
C2A
|
P:HEM502
|
4.2
|
76.7
|
1.0
|
|
C3C
|
P:HEM502
|
4.2
|
59.6
|
1.0
|
|
C3A
|
P:HEM502
|
4.2
|
71.7
|
1.0
|
|
C3B
|
P:HEM502
|
4.2
|
62.8
|
1.0
|
|
C2B
|
P:HEM502
|
4.3
|
76.0
|
1.0
|
|
O1A
|
P:HEM502
|
4.4
|
0.1
|
1.0
|
|
CA
|
P:GLY48
|
4.6
|
1.0
|
1.0
|
|
Iron binding site 8 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 8 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
Q:Fe501
b:81.5
occ:1.00
|
FE
|
Q:HEC501
|
0.0
|
81.5
|
1.0
|
|
NA
|
Q:HEC501
|
1.9
|
86.5
|
1.0
|
|
NC
|
Q:HEC501
|
1.9
|
0.5
|
1.0
|
|
NB
|
Q:HEC501
|
2.0
|
63.8
|
1.0
|
|
ND
|
Q:HEC501
|
2.0
|
74.9
|
1.0
|
|
NE2
|
Q:HIS38
|
2.0
|
75.0
|
1.0
|
|
SD
|
Q:MET183
|
2.1
|
68.9
|
1.0
|
|
C4A
|
Q:HEC501
|
2.9
|
0.7
|
1.0
|
|
CD2
|
Q:HIS38
|
2.9
|
70.2
|
1.0
|
|
C1A
|
Q:HEC501
|
3.0
|
0.7
|
1.0
|
|
C1C
|
Q:HEC501
|
3.0
|
0.3
|
1.0
|
|
C4C
|
Q:HEC501
|
3.0
|
0.1
|
1.0
|
|
CE1
|
Q:HIS38
|
3.0
|
57.8
|
1.0
|
|
C1B
|
Q:HEC501
|
3.0
|
86.9
|
1.0
|
|
C4B
|
Q:HEC501
|
3.0
|
89.4
|
1.0
|
|
C1D
|
Q:HEC501
|
3.0
|
90.5
|
1.0
|
|
C4D
|
Q:HEC501
|
3.0
|
84.4
|
1.0
|
|
CHB
|
Q:HEC501
|
3.3
|
0.8
|
1.0
|
|
CE
|
Q:MET183
|
3.3
|
74.9
|
1.0
|
|
CHC
|
Q:HEC501
|
3.3
|
0.5
|
1.0
|
|
CHD
|
Q:HEC501
|
3.3
|
0.5
|
1.0
|
|
CHA
|
Q:HEC501
|
3.4
|
99.1
|
1.0
|
|
CG
|
Q:MET183
|
3.5
|
54.3
|
1.0
|
|
ND1
|
Q:HIS38
|
4.1
|
81.7
|
1.0
|
|
CG
|
Q:HIS38
|
4.1
|
89.1
|
1.0
|
|
C3A
|
Q:HEC501
|
4.1
|
0.5
|
1.0
|
|
C2A
|
Q:HEC501
|
4.2
|
0.8
|
1.0
|
|
C2C
|
Q:HEC501
|
4.2
|
0.3
|
1.0
|
|
C3C
|
Q:HEC501
|
4.2
|
0.6
|
1.0
|
|
C2D
|
Q:HEC501
|
4.2
|
98.0
|
1.0
|
|
C3B
|
Q:HEC501
|
4.2
|
92.4
|
1.0
|
|
C2B
|
Q:HEC501
|
4.2
|
96.5
|
1.0
|
|
C3D
|
Q:HEC501
|
4.3
|
91.2
|
1.0
|
|
CB
|
Q:MET183
|
4.3
|
0.5
|
1.0
|
|
Iron binding site 9 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 9 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Fe501
b:0.0
occ:1.00
|
FE1
|
R:FES501
|
0.0
|
0.0
|
1.0
|
|
S1
|
R:FES501
|
2.2
|
0.9
|
1.0
|
|
S2
|
R:FES501
|
2.2
|
0.9
|
1.0
|
|
SG
|
R:CYS153
|
2.2
|
98.4
|
1.0
|
|
SG
|
R:CYS133
|
2.3
|
0.1
|
1.0
|
|
FE2
|
R:FES501
|
2.6
|
0.1
|
1.0
|
|
CB
|
R:CYS153
|
3.0
|
94.0
|
1.0
|
|
CB
|
R:CYS133
|
3.1
|
83.4
|
1.0
|
|
OG
|
R:SER158
|
3.2
|
97.4
|
1.0
|
|
CB
|
R:HIS135
|
4.0
|
0.5
|
1.0
|
|
CB
|
R:CYS155
|
4.1
|
0.4
|
1.0
|
|
ND1
|
R:HIS135
|
4.4
|
0.1
|
1.0
|
|
N
|
R:HIS156
|
4.4
|
79.4
|
1.0
|
|
ND1
|
R:HIS156
|
4.4
|
0.2
|
1.0
|
|
CA
|
R:CYS153
|
4.5
|
94.2
|
1.0
|
|
CB
|
R:SER158
|
4.5
|
0.8
|
1.0
|
|
CB
|
R:CYS138
|
4.5
|
0.8
|
1.0
|
|
N
|
R:LEU136
|
4.6
|
99.7
|
1.0
|
|
CA
|
R:CYS133
|
4.6
|
89.2
|
1.0
|
|
CG
|
R:HIS135
|
4.6
|
0.1
|
1.0
|
|
N
|
R:HIS135
|
4.8
|
0.2
|
1.0
|
|
N
|
R:CYS138
|
4.8
|
0.1
|
1.0
|
|
CA
|
R:CYS155
|
4.9
|
96.4
|
1.0
|
|
CA
|
R:HIS135
|
4.9
|
0.4
|
1.0
|
|
C
|
R:CYS153
|
4.9
|
93.4
|
1.0
|
|
N
|
R:CYS155
|
4.9
|
88.9
|
1.0
|
|
SG
|
R:CYS138
|
4.9
|
0.4
|
1.0
|
|
OH
|
R:TYR160
|
5.0
|
0.4
|
1.0
|
|
Iron binding site 10 out
of 10 in 1zrt
Go back to
Iron Binding Sites List in 1zrt
Iron binding site 10 out
of 10 in the Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Rhodobacter Capsulatus Cytochrome BC1 Complex with Stigmatellin Bound within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
R:Fe501
b:0.1
occ:1.00
|
FE2
|
R:FES501
|
0.0
|
0.1
|
1.0
|
|
ND1
|
R:HIS135
|
2.1
|
0.1
|
1.0
|
|
ND1
|
R:HIS156
|
2.1
|
0.2
|
1.0
|
|
S1
|
R:FES501
|
2.2
|
0.9
|
1.0
|
|
S2
|
R:FES501
|
2.2
|
0.9
|
1.0
|
|
FE1
|
R:FES501
|
2.6
|
0.0
|
1.0
|
|
CG
|
R:HIS135
|
3.0
|
0.1
|
1.0
|
|
CG
|
R:HIS156
|
3.0
|
73.5
|
1.0
|
|
CE1
|
R:HIS135
|
3.1
|
0.7
|
1.0
|
|
CE1
|
R:HIS156
|
3.2
|
0.7
|
1.0
|
|
CB
|
R:HIS156
|
3.3
|
57.7
|
1.0
|
|
CB
|
R:HIS135
|
3.3
|
0.5
|
1.0
|
|
N
|
R:HIS156
|
3.7
|
79.4
|
1.0
|
|
CB
|
R:CYS155
|
3.9
|
0.4
|
1.0
|
|
N
|
R:LEU136
|
4.1
|
99.7
|
1.0
|
|
CA
|
R:HIS156
|
4.1
|
83.3
|
1.0
|
|
CB
|
R:LEU136
|
4.1
|
96.9
|
1.0
|
|
CD2
|
R:HIS135
|
4.1
|
0.0
|
1.0
|
|
NE2
|
R:HIS135
|
4.2
|
0.5
|
1.0
|
|
CD2
|
R:HIS156
|
4.2
|
78.7
|
1.0
|
|
NE2
|
R:HIS156
|
4.2
|
95.5
|
1.0
|
|
C
|
R:CYS155
|
4.3
|
94.7
|
1.0
|
|
SG
|
R:CYS153
|
4.4
|
98.4
|
1.0
|
|
SG
|
R:CYS133
|
4.4
|
0.1
|
1.0
|
|
C
|
R:HIS135
|
4.4
|
0.3
|
1.0
|
|
CA
|
R:HIS135
|
4.5
|
0.4
|
1.0
|
|
CA
|
R:CYS155
|
4.7
|
96.4
|
1.0
|
|
CA
|
R:LEU136
|
4.7
|
99.6
|
1.0
|
|
OG
|
R:SER158
|
4.7
|
97.4
|
1.0
|
|
CG
|
R:LEU136
|
4.8
|
0.2
|
1.0
|
|
CD1
|
R:LEU136
|
4.9
|
0.2
|
1.0
|
|
O
|
R:CYS155
|
5.0
|
96.4
|
1.0
|
|
Reference:
E.A.Berry,
L.S.Huang,
L.K.Saechao,
N.G.Pon,
M.Valkova-Valchanova,
F.Daldal.
X-Ray Structure of Rhodobacter Capsulatus Cytochrome Bc (1): Comparison with Its Mitochondrial and Chloroplast Counterparts. Photosynth.Res. V. 81 251 2004.
ISSN: ISSN 0166-8595
PubMed: 16034531
DOI: 10.1023/B:PRES.0000036888.18223.0E
Page generated: Sun Dec 13 14:39:03 2020
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