Iron in PDB 2bs2: Quinol:Fumarate Reductase From Wolinella Succinogenes
Enzymatic activity of Quinol:Fumarate Reductase From Wolinella Succinogenes
All present enzymatic activity of Quinol:Fumarate Reductase From Wolinella Succinogenes:
1.3.99.1;
Protein crystallography data
The structure of Quinol:Fumarate Reductase From Wolinella Succinogenes, PDB code: 2bs2
was solved by
C.R.D.Lancaster,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
28.70 /
1.78
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.104,
188.766,
117.817,
90.00,
104.47,
90.00
|
R / Rfree (%)
|
22.9 /
23.7
|
Other elements in 2bs2:
The structure of Quinol:Fumarate Reductase From Wolinella Succinogenes also contains other interesting chemical elements:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
22;
Binding sites:
The binding sites of Iron atom in the Quinol:Fumarate Reductase From Wolinella Succinogenes
(pdb code 2bs2). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 22 binding sites of Iron where determined in the
Quinol:Fumarate Reductase From Wolinella Succinogenes, PDB code: 2bs2:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 1 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1240
b:22.8
occ:1.00
|
FE1
|
B:FES1240
|
0.0
|
22.8
|
1.0
|
SG
|
B:CYS65
|
2.1
|
23.7
|
1.0
|
S1
|
B:FES1240
|
2.2
|
23.6
|
1.0
|
SG
|
B:CYS77
|
2.2
|
26.8
|
1.0
|
S2
|
B:FES1240
|
2.2
|
24.1
|
1.0
|
FE2
|
B:FES1240
|
2.7
|
22.7
|
1.0
|
CB
|
B:CYS77
|
3.3
|
26.8
|
1.0
|
CB
|
B:CYS65
|
3.4
|
21.7
|
1.0
|
N
|
B:CYS65
|
3.9
|
22.0
|
1.0
|
N
|
B:GLY60
|
4.2
|
26.1
|
1.0
|
SG
|
B:CYS57
|
4.2
|
22.9
|
1.0
|
N
|
B:CYS77
|
4.3
|
26.0
|
1.0
|
CA
|
B:CYS65
|
4.3
|
22.6
|
1.0
|
CA
|
B:CYS77
|
4.4
|
28.9
|
1.0
|
CA
|
B:GLY60
|
4.5
|
25.4
|
1.0
|
N
|
B:ARG58
|
4.5
|
25.1
|
1.0
|
CD1
|
B:PHE55
|
4.6
|
24.2
|
1.0
|
CA
|
B:ARG58
|
4.6
|
25.6
|
1.0
|
SG
|
B:CYS62
|
4.7
|
23.1
|
1.0
|
CB
|
B:LEU75
|
4.7
|
26.3
|
1.0
|
N
|
B:SER64
|
4.7
|
20.0
|
1.0
|
CD2
|
B:LEU75
|
4.8
|
26.7
|
1.0
|
N
|
B:ALA59
|
4.8
|
26.1
|
1.0
|
CE1
|
B:PHE55
|
4.9
|
22.2
|
1.0
|
C
|
B:ARG58
|
5.0
|
27.2
|
1.0
|
|
Iron binding site 2 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 2 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1240
b:22.7
occ:1.00
|
FE2
|
B:FES1240
|
0.0
|
22.7
|
1.0
|
S1
|
B:FES1240
|
2.2
|
23.6
|
1.0
|
SG
|
B:CYS62
|
2.2
|
23.1
|
1.0
|
S2
|
B:FES1240
|
2.2
|
24.1
|
1.0
|
SG
|
B:CYS57
|
2.2
|
22.9
|
1.0
|
FE1
|
B:FES1240
|
2.7
|
22.8
|
1.0
|
CB
|
B:CYS62
|
3.4
|
24.1
|
1.0
|
CB
|
B:CYS57
|
3.5
|
22.1
|
1.0
|
N
|
B:CYS62
|
3.6
|
25.9
|
1.0
|
N
|
B:CYS57
|
3.6
|
22.6
|
1.0
|
N
|
B:ARG58
|
3.8
|
25.1
|
1.0
|
N
|
B:GLY63
|
3.8
|
22.4
|
1.0
|
CA
|
B:CYS62
|
3.9
|
24.4
|
1.0
|
CA
|
B:CYS57
|
4.0
|
22.9
|
1.0
|
N
|
B:SER64
|
4.0
|
20.0
|
1.0
|
C
|
B:CYS62
|
4.2
|
23.0
|
1.0
|
SG
|
B:CYS77
|
4.3
|
26.8
|
1.0
|
C
|
B:CYS57
|
4.3
|
24.7
|
1.0
|
CB
|
B:SER64
|
4.3
|
22.9
|
1.0
|
N
|
B:GLY60
|
4.3
|
26.1
|
1.0
|
N
|
B:ILE61
|
4.4
|
25.1
|
1.0
|
SG
|
B:CYS65
|
4.6
|
23.7
|
1.0
|
N
|
B:VAL56
|
4.6
|
22.3
|
1.0
|
N
|
B:ALA59
|
4.6
|
26.1
|
1.0
|
C
|
B:VAL56
|
4.7
|
22.3
|
1.0
|
CA
|
B:ARG58
|
4.7
|
25.6
|
1.0
|
CA
|
B:SER64
|
4.7
|
21.3
|
1.0
|
CA
|
B:GLY60
|
4.7
|
25.4
|
1.0
|
C
|
B:ILE61
|
4.8
|
26.5
|
1.0
|
CA
|
B:GLY63
|
4.8
|
21.6
|
1.0
|
N
|
B:CYS65
|
4.8
|
22.0
|
1.0
|
CB
|
B:VAL56
|
4.8
|
22.4
|
1.0
|
C
|
B:GLY63
|
4.9
|
22.8
|
1.0
|
C
|
B:GLY60
|
4.9
|
25.8
|
1.0
|
CA
|
B:VAL56
|
4.9
|
21.2
|
1.0
|
|
Iron binding site 3 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 3 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1241
b:25.7
occ:1.00
|
FE1
|
B:F3S1241
|
0.0
|
25.7
|
1.0
|
SG
|
B:CYS161
|
2.2
|
24.6
|
1.0
|
S1
|
B:F3S1241
|
2.2
|
27.0
|
1.0
|
S2
|
B:F3S1241
|
2.3
|
25.2
|
1.0
|
S3
|
B:F3S1241
|
2.3
|
24.7
|
1.0
|
FE3
|
B:F3S1241
|
2.7
|
24.7
|
1.0
|
FE4
|
B:F3S1241
|
2.8
|
25.5
|
1.0
|
CB
|
B:CYS161
|
3.4
|
25.4
|
1.0
|
S4
|
B:F3S1241
|
3.8
|
26.8
|
1.0
|
CA
|
B:CYS161
|
4.1
|
25.6
|
1.0
|
CE2
|
B:PHE170
|
4.1
|
25.9
|
1.0
|
O
|
B:HOH2104
|
4.1
|
21.8
|
1.0
|
OG1
|
B:THR163
|
4.3
|
25.7
|
1.0
|
CB
|
B:THR163
|
4.5
|
25.5
|
1.0
|
CB
|
B:LEU211
|
4.6
|
25.7
|
1.0
|
CD1
|
B:LEU211
|
4.7
|
25.2
|
1.0
|
CZ
|
B:PHE170
|
4.7
|
25.7
|
1.0
|
SG
|
B:CYS214
|
4.8
|
23.1
|
1.0
|
SG
|
B:CYS208
|
4.8
|
24.6
|
1.0
|
CG
|
B:LEU211
|
4.8
|
25.6
|
1.0
|
C
|
B:CYS161
|
4.8
|
25.8
|
1.0
|
N
|
B:LEU211
|
4.9
|
27.9
|
1.0
|
N
|
B:THR163
|
5.0
|
24.9
|
1.0
|
|
Iron binding site 4 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 4 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1241
b:24.7
occ:1.00
|
FE3
|
B:F3S1241
|
0.0
|
24.7
|
1.0
|
SG
|
B:CYS208
|
2.1
|
24.6
|
1.0
|
S1
|
B:F3S1241
|
2.3
|
27.0
|
1.0
|
S4
|
B:F3S1241
|
2.3
|
26.8
|
1.0
|
S3
|
B:F3S1241
|
2.3
|
24.7
|
1.0
|
FE1
|
B:F3S1241
|
2.7
|
25.7
|
1.0
|
FE4
|
B:F3S1241
|
2.8
|
25.5
|
1.0
|
CB
|
B:CYS208
|
3.5
|
25.9
|
1.0
|
N
|
B:THR210
|
3.8
|
27.5
|
1.0
|
CA
|
B:CYS208
|
3.9
|
26.4
|
1.0
|
S2
|
B:F3S1241
|
4.0
|
25.2
|
1.0
|
N
|
B:MET209
|
4.0
|
26.7
|
1.0
|
CA
|
B:THR210
|
4.2
|
26.7
|
1.0
|
N
|
B:LEU211
|
4.3
|
27.9
|
1.0
|
C
|
B:CYS208
|
4.3
|
26.8
|
1.0
|
O
|
B:HOH2142
|
4.4
|
25.9
|
1.0
|
CZ
|
B:PHE170
|
4.4
|
25.7
|
1.0
|
CE2
|
B:PHE170
|
4.6
|
25.9
|
1.0
|
SG
|
B:CYS161
|
4.7
|
24.6
|
1.0
|
SG
|
B:CYS214
|
4.7
|
23.1
|
1.0
|
C
|
B:THR210
|
4.8
|
28.0
|
1.0
|
C
|
B:MET209
|
4.8
|
27.3
|
1.0
|
CD1
|
B:ILE228
|
4.8
|
28.6
|
1.0
|
N
|
B:LEU212
|
5.0
|
26.6
|
1.0
|
|
Iron binding site 5 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 5 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1241
b:25.5
occ:1.00
|
FE4
|
B:F3S1241
|
0.0
|
25.5
|
1.0
|
SG
|
B:CYS214
|
2.1
|
23.1
|
1.0
|
S4
|
B:F3S1241
|
2.2
|
26.8
|
1.0
|
S3
|
B:F3S1241
|
2.2
|
24.7
|
1.0
|
S2
|
B:F3S1241
|
2.3
|
25.2
|
1.0
|
FE1
|
B:F3S1241
|
2.8
|
25.7
|
1.0
|
FE3
|
B:F3S1241
|
2.8
|
24.7
|
1.0
|
CB
|
B:CYS214
|
3.2
|
23.2
|
1.0
|
S1
|
B:F3S1241
|
3.9
|
27.0
|
1.0
|
N
|
B:CYS214
|
3.9
|
24.6
|
1.0
|
N
|
B:LEU212
|
4.1
|
26.6
|
1.0
|
CA
|
B:CYS214
|
4.2
|
23.9
|
1.0
|
CA
|
B:LEU212
|
4.2
|
27.5
|
1.0
|
CB
|
B:ALA173
|
4.3
|
23.9
|
1.0
|
CD1
|
B:ILE228
|
4.5
|
28.6
|
1.0
|
N
|
B:ALA213
|
4.5
|
26.6
|
1.0
|
C
|
B:LEU212
|
4.6
|
27.1
|
1.0
|
SG
|
B:CYS208
|
4.6
|
24.6
|
1.0
|
SG
|
B:CYS161
|
4.7
|
24.6
|
1.0
|
N
|
B:LEU211
|
4.9
|
27.9
|
1.0
|
O
|
B:HOH2104
|
4.9
|
21.8
|
1.0
|
N
|
B:HIS215
|
5.0
|
26.0
|
1.0
|
|
Iron binding site 6 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 6 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1242
b:25.2
occ:1.00
|
FE1
|
B:SF41242
|
0.0
|
25.2
|
1.0
|
SG
|
B:CYS157
|
2.1
|
24.5
|
1.0
|
S2
|
B:SF41242
|
2.3
|
24.6
|
1.0
|
S3
|
B:SF41242
|
2.3
|
24.0
|
1.0
|
S4
|
B:SF41242
|
2.3
|
22.2
|
1.0
|
FE4
|
B:SF41242
|
2.7
|
25.0
|
1.0
|
FE3
|
B:SF41242
|
2.8
|
25.2
|
1.0
|
FE2
|
B:SF41242
|
2.8
|
24.5
|
1.0
|
CB
|
B:CYS157
|
3.2
|
23.9
|
1.0
|
S1
|
B:SF41242
|
3.9
|
24.4
|
1.0
|
N
|
B:CYS157
|
3.9
|
22.7
|
1.0
|
CA
|
B:CYS157
|
4.2
|
24.3
|
1.0
|
CB
|
B:ALA174
|
4.2
|
24.6
|
1.0
|
SG
|
B:CYS151
|
4.6
|
24.0
|
1.0
|
SG
|
B:CYS154
|
4.6
|
26.1
|
1.0
|
SG
|
B:CYS218
|
4.7
|
27.2
|
1.0
|
CA
|
B:ALA174
|
4.7
|
24.3
|
1.0
|
N
|
B:ALA174
|
4.8
|
24.9
|
1.0
|
N
|
B:CYS156
|
4.9
|
20.9
|
1.0
|
N
|
B:GLY155
|
5.0
|
22.0
|
1.0
|
|
Iron binding site 7 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 7 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1242
b:24.5
occ:1.00
|
FE2
|
B:SF41242
|
0.0
|
24.5
|
1.0
|
SG
|
B:CYS154
|
2.2
|
26.1
|
1.0
|
S3
|
B:SF41242
|
2.3
|
24.0
|
1.0
|
S4
|
B:SF41242
|
2.3
|
22.2
|
1.0
|
S1
|
B:SF41242
|
2.3
|
24.4
|
1.0
|
FE3
|
B:SF41242
|
2.7
|
25.2
|
1.0
|
FE4
|
B:SF41242
|
2.8
|
25.0
|
1.0
|
FE1
|
B:SF41242
|
2.8
|
25.2
|
1.0
|
N
|
B:CYS154
|
3.6
|
21.7
|
1.0
|
CB
|
B:CYS154
|
3.6
|
20.8
|
1.0
|
S2
|
B:SF41242
|
3.9
|
24.6
|
1.0
|
N
|
B:GLY155
|
4.0
|
22.0
|
1.0
|
CA
|
B:CYS154
|
4.0
|
21.7
|
1.0
|
CD
|
B:PRO219
|
4.3
|
27.3
|
1.0
|
N
|
B:CYS156
|
4.3
|
20.9
|
1.0
|
C
|
B:CYS154
|
4.4
|
21.0
|
1.0
|
N
|
B:GLU153
|
4.5
|
21.9
|
1.0
|
CG1
|
B:ILE152
|
4.6
|
21.2
|
1.0
|
SG
|
B:CYS151
|
4.6
|
24.0
|
1.0
|
C
|
B:GLU153
|
4.6
|
22.6
|
1.0
|
CG
|
B:PRO219
|
4.6
|
31.2
|
1.0
|
SG
|
B:CYS218
|
4.6
|
27.2
|
1.0
|
SG
|
B:CYS157
|
4.6
|
24.5
|
1.0
|
CA
|
B:GLU153
|
4.8
|
22.9
|
1.0
|
CB
|
B:CYS156
|
4.8
|
23.4
|
1.0
|
N
|
B:CYS157
|
4.8
|
22.7
|
1.0
|
N
|
B:ILE152
|
4.9
|
23.3
|
1.0
|
CA
|
B:GLY155
|
5.0
|
22.3
|
1.0
|
|
Iron binding site 8 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 8 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1242
b:25.2
occ:1.00
|
FE3
|
B:SF41242
|
0.0
|
25.2
|
1.0
|
SG
|
B:CYS151
|
2.2
|
24.0
|
1.0
|
S1
|
B:SF41242
|
2.2
|
24.4
|
1.0
|
S4
|
B:SF41242
|
2.2
|
22.2
|
1.0
|
S2
|
B:SF41242
|
2.2
|
24.6
|
1.0
|
FE2
|
B:SF41242
|
2.7
|
24.5
|
1.0
|
FE1
|
B:SF41242
|
2.8
|
25.2
|
1.0
|
FE4
|
B:SF41242
|
2.8
|
25.0
|
1.0
|
CB
|
B:CYS151
|
3.3
|
23.0
|
1.0
|
CA
|
B:CYS151
|
3.7
|
22.6
|
1.0
|
S3
|
B:SF41242
|
3.9
|
24.0
|
1.0
|
N
|
B:ILE152
|
3.9
|
23.3
|
1.0
|
N
|
B:GLU153
|
4.0
|
21.9
|
1.0
|
C
|
B:CYS151
|
4.2
|
23.7
|
1.0
|
CA
|
B:GLU153
|
4.5
|
22.9
|
1.0
|
CB
|
B:ALA174
|
4.7
|
24.6
|
1.0
|
SG
|
B:CYS157
|
4.7
|
24.5
|
1.0
|
N
|
B:CYS154
|
4.7
|
21.7
|
1.0
|
SG
|
B:CYS218
|
4.8
|
27.2
|
1.0
|
CD2
|
B:LEU222
|
4.8
|
30.4
|
1.0
|
O
|
B:HOH2114
|
4.8
|
22.6
|
1.0
|
SG
|
B:CYS154
|
4.8
|
26.1
|
1.0
|
C
|
B:ILE152
|
4.9
|
23.0
|
1.0
|
CA
|
B:ILE152
|
5.0
|
21.5
|
1.0
|
|
Iron binding site 9 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 9 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe1242
b:25.0
occ:1.00
|
FE4
|
B:SF41242
|
0.0
|
25.0
|
1.0
|
SG
|
B:CYS218
|
2.2
|
27.2
|
1.0
|
S3
|
B:SF41242
|
2.3
|
24.0
|
1.0
|
S2
|
B:SF41242
|
2.3
|
24.6
|
1.0
|
S1
|
B:SF41242
|
2.3
|
24.4
|
1.0
|
FE1
|
B:SF41242
|
2.7
|
25.2
|
1.0
|
FE2
|
B:SF41242
|
2.8
|
24.5
|
1.0
|
FE3
|
B:SF41242
|
2.8
|
25.2
|
1.0
|
CB
|
B:CYS218
|
3.4
|
26.5
|
1.0
|
CA
|
B:CYS218
|
3.9
|
25.7
|
1.0
|
S4
|
B:SF41242
|
3.9
|
22.2
|
1.0
|
CD
|
B:PRO219
|
4.3
|
27.3
|
1.0
|
C
|
B:CYS218
|
4.6
|
28.0
|
1.0
|
SG
|
B:CYS157
|
4.6
|
24.5
|
1.0
|
SG
|
B:CYS154
|
4.6
|
26.1
|
1.0
|
N
|
B:PRO219
|
4.7
|
29.5
|
1.0
|
CD1
|
B:LEU224
|
4.7
|
21.4
|
1.0
|
CD2
|
B:LEU222
|
4.8
|
30.4
|
1.0
|
CD1
|
B:LEU222
|
4.8
|
31.2
|
1.0
|
SG
|
B:CYS151
|
4.9
|
24.0
|
1.0
|
CB
|
B:CYS157
|
4.9
|
23.9
|
1.0
|
N
|
B:LYS220
|
5.0
|
29.0
|
1.0
|
|
Iron binding site 10 out
of 22 in 2bs2
Go back to
Iron Binding Sites List in 2bs2
Iron binding site 10 out
of 22 in the Quinol:Fumarate Reductase From Wolinella Succinogenes
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe1255
b:29.8
occ:1.00
|
FE
|
C:HEM1255
|
0.0
|
29.8
|
1.0
|
NA
|
C:HEM1255
|
2.0
|
30.9
|
1.0
|
NE2
|
C:HIS93
|
2.0
|
29.7
|
1.0
|
NE2
|
C:HIS182
|
2.0
|
30.5
|
1.0
|
NB
|
C:HEM1255
|
2.0
|
32.3
|
1.0
|
ND
|
C:HEM1255
|
2.0
|
29.8
|
1.0
|
NC
|
C:HEM1255
|
2.1
|
32.2
|
1.0
|
CD2
|
C:HIS182
|
3.0
|
32.8
|
1.0
|
CD2
|
C:HIS93
|
3.0
|
28.3
|
1.0
|
C1A
|
C:HEM1255
|
3.0
|
32.2
|
1.0
|
CE1
|
C:HIS93
|
3.0
|
29.4
|
1.0
|
C4A
|
C:HEM1255
|
3.0
|
31.2
|
1.0
|
CE1
|
C:HIS182
|
3.0
|
30.6
|
1.0
|
C1B
|
C:HEM1255
|
3.1
|
32.6
|
1.0
|
C4D
|
C:HEM1255
|
3.1
|
31.0
|
1.0
|
C4B
|
C:HEM1255
|
3.1
|
33.9
|
1.0
|
C1D
|
C:HEM1255
|
3.1
|
30.8
|
1.0
|
C1C
|
C:HEM1255
|
3.1
|
32.1
|
1.0
|
C4C
|
C:HEM1255
|
3.1
|
31.7
|
1.0
|
CHB
|
C:HEM1255
|
3.4
|
31.1
|
1.0
|
CHA
|
C:HEM1255
|
3.4
|
30.9
|
1.0
|
CHC
|
C:HEM1255
|
3.5
|
33.8
|
1.0
|
CHD
|
C:HEM1255
|
3.5
|
30.9
|
1.0
|
ND1
|
C:HIS93
|
4.1
|
28.9
|
1.0
|
ND1
|
C:HIS182
|
4.1
|
32.2
|
1.0
|
CG
|
C:HIS182
|
4.1
|
32.8
|
1.0
|
CG
|
C:HIS93
|
4.1
|
29.9
|
1.0
|
C2A
|
C:HEM1255
|
4.2
|
31.7
|
1.0
|
C3A
|
C:HEM1255
|
4.2
|
32.3
|
1.0
|
C2B
|
C:HEM1255
|
4.3
|
31.8
|
1.0
|
C3B
|
C:HEM1255
|
4.3
|
33.6
|
1.0
|
C3D
|
C:HEM1255
|
4.3
|
29.2
|
1.0
|
C2D
|
C:HEM1255
|
4.3
|
30.2
|
1.0
|
O
|
C:HOH2045
|
4.3
|
28.0
|
1.0
|
C3C
|
C:HEM1255
|
4.3
|
31.8
|
1.0
|
C2C
|
C:HEM1255
|
4.3
|
32.4
|
1.0
|
|
Reference:
M.G.Madej,
H.R.Nasiri,
N.S.Hilgendorff,
H.Schwalbe,
C.R.D.Lancaster.
Evidence For Transmembrane Proton Transfer in A Dihaem-Containing Membrane Protein Complex. Embo J. V. 25 4963 2006.
ISSN: ISSN 0261-4189
PubMed: 17024183
DOI: 10.1038/SJ.EMBOJ.7601361
Page generated: Sat Aug 3 19:46:34 2024
|