Iron in PDB 2gmh: Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
Enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
All present enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone:
1.5.5.1;
Protein crystallography data
The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh
was solved by
J.Zhang,
F.E.Frerman,
J.-J.P.Kim,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.67 /
2.50
|
Space group
|
P 4 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
154.322,
154.322,
128.536,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.1 /
25.4
|
Other elements in 2gmh:
The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
(pdb code 2gmh). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the
Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone, PDB code: 2gmh:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 1 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:19.3
occ:1.00
|
FE1
|
A:SF4610
|
0.0
|
19.3
|
1.0
|
S2
|
A:SF4610
|
2.3
|
19.4
|
1.0
|
S4
|
A:SF4610
|
2.3
|
19.3
|
1.0
|
S3
|
A:SF4610
|
2.3
|
16.7
|
1.0
|
SG
|
A:CYS553
|
2.3
|
23.1
|
1.0
|
FE4
|
A:SF4610
|
2.7
|
22.5
|
1.0
|
FE2
|
A:SF4610
|
2.7
|
18.0
|
1.0
|
FE3
|
A:SF4610
|
2.8
|
22.7
|
1.0
|
CB
|
A:CYS553
|
3.4
|
26.8
|
1.0
|
CA
|
A:CYS553
|
3.7
|
26.1
|
1.0
|
S1
|
A:SF4610
|
3.9
|
18.0
|
1.0
|
N
|
A:VAL554
|
3.9
|
23.1
|
1.0
|
N
|
A:HIS555
|
4.0
|
19.4
|
1.0
|
CD1
|
A:LEU504
|
4.2
|
29.6
|
1.0
|
C
|
A:CYS553
|
4.2
|
26.5
|
1.0
|
NE1
|
A:TRP570
|
4.4
|
22.5
|
1.0
|
CG2
|
A:VAL532
|
4.4
|
25.6
|
1.0
|
CA
|
A:HIS555
|
4.5
|
21.6
|
1.0
|
N
|
A:CYS556
|
4.6
|
19.7
|
1.0
|
CD1
|
A:TRP570
|
4.7
|
21.2
|
1.0
|
SG
|
A:CYS528
|
4.8
|
20.5
|
1.0
|
SG
|
A:CYS556
|
4.8
|
22.3
|
1.0
|
SG
|
A:CYS559
|
4.9
|
20.5
|
1.0
|
CG
|
A:LEU504
|
4.9
|
32.3
|
1.0
|
C
|
A:VAL554
|
4.9
|
20.1
|
1.0
|
N
|
A:CYS553
|
4.9
|
24.6
|
1.0
|
CD2
|
A:LEU504
|
4.9
|
30.0
|
1.0
|
CA
|
A:VAL554
|
5.0
|
21.0
|
1.0
|
|
Iron binding site 2 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 2 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:18.0
occ:1.00
|
FE2
|
A:SF4610
|
0.0
|
18.0
|
1.0
|
SG
|
A:CYS528
|
2.2
|
20.5
|
1.0
|
S1
|
A:SF4610
|
2.3
|
18.0
|
1.0
|
S4
|
A:SF4610
|
2.3
|
19.3
|
1.0
|
S3
|
A:SF4610
|
2.3
|
16.7
|
1.0
|
FE4
|
A:SF4610
|
2.7
|
22.5
|
1.0
|
FE1
|
A:SF4610
|
2.7
|
19.3
|
1.0
|
FE3
|
A:SF4610
|
2.8
|
22.7
|
1.0
|
CB
|
A:CYS528
|
3.4
|
23.7
|
1.0
|
S2
|
A:SF4610
|
3.8
|
19.4
|
1.0
|
CD
|
A:PRO529
|
3.9
|
24.2
|
1.0
|
CA
|
A:CYS528
|
4.0
|
25.8
|
1.0
|
CG2
|
A:VAL532
|
4.0
|
25.6
|
1.0
|
CB
|
A:VAL532
|
4.2
|
23.4
|
1.0
|
N
|
A:PRO529
|
4.5
|
26.0
|
1.0
|
C
|
A:CYS528
|
4.5
|
25.4
|
1.0
|
CB
|
A:ALA530
|
4.6
|
16.8
|
1.0
|
CE1
|
A:TYR533
|
4.6
|
17.8
|
1.0
|
N
|
A:ALA530
|
4.6
|
22.3
|
1.0
|
SG
|
A:CYS556
|
4.7
|
22.3
|
1.0
|
CG
|
A:PRO529
|
4.7
|
21.8
|
1.0
|
SG
|
A:CYS559
|
4.7
|
20.5
|
1.0
|
SG
|
A:CYS553
|
5.0
|
23.1
|
1.0
|
|
Iron binding site 3 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 3 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:22.7
occ:1.00
|
FE3
|
A:SF4610
|
0.0
|
22.7
|
1.0
|
S4
|
A:SF4610
|
2.2
|
19.3
|
1.0
|
SG
|
A:CYS556
|
2.2
|
22.3
|
1.0
|
S2
|
A:SF4610
|
2.3
|
19.4
|
1.0
|
S1
|
A:SF4610
|
2.3
|
18.0
|
1.0
|
FE4
|
A:SF4610
|
2.7
|
22.5
|
1.0
|
FE2
|
A:SF4610
|
2.8
|
18.0
|
1.0
|
FE1
|
A:SF4610
|
2.8
|
19.3
|
1.0
|
N
|
A:CYS556
|
3.6
|
19.7
|
1.0
|
CB
|
A:CYS556
|
3.6
|
20.7
|
1.0
|
N
|
A:LYS557
|
3.8
|
18.6
|
1.0
|
S3
|
A:SF4610
|
3.9
|
16.7
|
1.0
|
CD
|
A:PRO529
|
3.9
|
24.2
|
1.0
|
CA
|
A:CYS556
|
4.0
|
21.6
|
1.0
|
N
|
A:THR558
|
4.0
|
20.4
|
1.0
|
CG
|
A:PRO529
|
4.2
|
21.8
|
1.0
|
C
|
A:CYS556
|
4.4
|
20.5
|
1.0
|
CB
|
A:THR558
|
4.5
|
17.4
|
1.0
|
C
|
A:HIS555
|
4.6
|
20.8
|
1.0
|
CA
|
A:LYS557
|
4.7
|
17.8
|
1.0
|
SG
|
A:CYS528
|
4.7
|
20.5
|
1.0
|
CG2
|
A:VAL554
|
4.7
|
19.1
|
1.0
|
N
|
A:HIS555
|
4.7
|
19.4
|
1.0
|
SG
|
A:CYS559
|
4.7
|
20.5
|
1.0
|
N
|
A:CYS559
|
4.7
|
21.6
|
1.0
|
OG1
|
A:THR558
|
4.8
|
21.5
|
1.0
|
SG
|
A:CYS553
|
4.8
|
23.1
|
1.0
|
C
|
A:LYS557
|
4.8
|
20.7
|
1.0
|
CA
|
A:THR558
|
4.8
|
19.9
|
1.0
|
CA
|
A:HIS555
|
4.9
|
21.6
|
1.0
|
|
Iron binding site 4 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 4 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:22.5
occ:1.00
|
FE4
|
A:SF4610
|
0.0
|
22.5
|
1.0
|
S2
|
A:SF4610
|
2.2
|
19.4
|
1.0
|
S1
|
A:SF4610
|
2.2
|
18.0
|
1.0
|
S3
|
A:SF4610
|
2.2
|
16.7
|
1.0
|
SG
|
A:CYS559
|
2.3
|
20.5
|
1.0
|
FE3
|
A:SF4610
|
2.7
|
22.7
|
1.0
|
FE1
|
A:SF4610
|
2.7
|
19.3
|
1.0
|
FE2
|
A:SF4610
|
2.7
|
18.0
|
1.0
|
CB
|
A:CYS559
|
3.3
|
19.6
|
1.0
|
S4
|
A:SF4610
|
3.8
|
19.3
|
1.0
|
N
|
A:CYS559
|
3.8
|
21.6
|
1.0
|
CD1
|
A:LEU504
|
3.9
|
29.6
|
1.0
|
CA
|
A:CYS559
|
4.2
|
21.7
|
1.0
|
OH
|
A:TYR533
|
4.3
|
21.3
|
1.0
|
CE1
|
A:TYR533
|
4.4
|
17.8
|
1.0
|
CD1
|
A:TRP570
|
4.6
|
21.2
|
1.0
|
SG
|
A:CYS556
|
4.6
|
22.3
|
1.0
|
N
|
A:THR558
|
4.6
|
20.4
|
1.0
|
SG
|
A:CYS553
|
4.7
|
23.1
|
1.0
|
SG
|
A:CYS528
|
4.7
|
20.5
|
1.0
|
CG
|
A:LEU504
|
4.8
|
32.3
|
1.0
|
CZ
|
A:TYR533
|
4.8
|
22.5
|
1.0
|
C
|
A:THR558
|
5.0
|
21.3
|
1.0
|
N
|
A:LYS557
|
5.0
|
18.6
|
1.0
|
|
Iron binding site 5 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 5 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe613
b:59.8
occ:1.00
|
FE1
|
B:SF4613
|
0.0
|
59.8
|
1.0
|
S2
|
B:SF4613
|
2.3
|
57.4
|
1.0
|
S4
|
B:SF4613
|
2.3
|
58.4
|
1.0
|
S3
|
B:SF4613
|
2.3
|
59.0
|
1.0
|
SG
|
B:CYS553
|
2.5
|
69.5
|
1.0
|
FE4
|
B:SF4613
|
2.7
|
59.3
|
1.0
|
FE3
|
B:SF4613
|
2.8
|
59.8
|
1.0
|
FE2
|
B:SF4613
|
2.8
|
59.2
|
1.0
|
CB
|
B:CYS553
|
3.1
|
67.7
|
1.0
|
CA
|
B:CYS553
|
3.3
|
67.6
|
1.0
|
N
|
B:VAL554
|
3.7
|
66.4
|
1.0
|
S1
|
B:SF4613
|
3.9
|
56.0
|
1.0
|
C
|
B:CYS553
|
3.9
|
67.2
|
1.0
|
N
|
B:HIS555
|
4.1
|
64.4
|
1.0
|
CG2
|
B:VAL532
|
4.4
|
67.4
|
1.0
|
N
|
B:CYS553
|
4.5
|
67.6
|
1.0
|
N
|
B:CYS556
|
4.6
|
61.9
|
1.0
|
NE1
|
B:TRP570
|
4.7
|
53.5
|
1.0
|
CA
|
B:HIS555
|
4.7
|
63.9
|
1.0
|
CD1
|
B:LEU504
|
4.8
|
66.5
|
1.0
|
CD1
|
B:TRP570
|
4.8
|
54.4
|
1.0
|
SG
|
B:CYS528
|
4.8
|
53.4
|
1.0
|
SG
|
B:CYS556
|
4.9
|
66.8
|
1.0
|
CA
|
B:VAL554
|
4.9
|
65.8
|
1.0
|
SG
|
B:CYS559
|
4.9
|
52.2
|
1.0
|
C
|
B:VAL554
|
4.9
|
65.3
|
1.0
|
O
|
B:CYS553
|
4.9
|
67.6
|
1.0
|
|
Iron binding site 6 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 6 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe613
b:59.2
occ:1.00
|
FE2
|
B:SF4613
|
0.0
|
59.2
|
1.0
|
SG
|
B:CYS528
|
2.3
|
53.4
|
1.0
|
S1
|
B:SF4613
|
2.3
|
56.0
|
1.0
|
S3
|
B:SF4613
|
2.3
|
59.0
|
1.0
|
S4
|
B:SF4613
|
2.3
|
58.4
|
1.0
|
FE4
|
B:SF4613
|
2.7
|
59.3
|
1.0
|
FE1
|
B:SF4613
|
2.8
|
59.8
|
1.0
|
FE3
|
B:SF4613
|
2.8
|
59.8
|
1.0
|
CB
|
B:CYS528
|
3.6
|
57.3
|
1.0
|
CD
|
B:PRO529
|
3.7
|
59.0
|
1.0
|
S2
|
B:SF4613
|
3.9
|
57.4
|
1.0
|
CG2
|
B:VAL532
|
4.0
|
67.4
|
1.0
|
CA
|
B:CYS528
|
4.1
|
57.6
|
1.0
|
CE1
|
B:TYR533
|
4.3
|
69.8
|
1.0
|
CB
|
B:VAL532
|
4.4
|
68.3
|
1.0
|
CG
|
B:PRO529
|
4.5
|
59.5
|
1.0
|
N
|
B:PRO529
|
4.5
|
58.9
|
1.0
|
CB
|
B:ALA530
|
4.6
|
63.7
|
1.0
|
N
|
B:ALA530
|
4.6
|
63.9
|
1.0
|
C
|
B:CYS528
|
4.6
|
58.1
|
1.0
|
SG
|
B:CYS559
|
4.7
|
52.2
|
1.0
|
SG
|
B:CYS556
|
4.7
|
66.8
|
1.0
|
CA
|
B:CYS553
|
4.9
|
67.6
|
1.0
|
CD1
|
B:TYR533
|
4.9
|
69.8
|
1.0
|
|
Iron binding site 7 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 7 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe613
b:59.8
occ:1.00
|
FE3
|
B:SF4613
|
0.0
|
59.8
|
1.0
|
S4
|
B:SF4613
|
2.2
|
58.4
|
1.0
|
SG
|
B:CYS556
|
2.3
|
66.8
|
1.0
|
S2
|
B:SF4613
|
2.3
|
57.4
|
1.0
|
S1
|
B:SF4613
|
2.3
|
56.0
|
1.0
|
FE4
|
B:SF4613
|
2.7
|
59.3
|
1.0
|
FE1
|
B:SF4613
|
2.8
|
59.8
|
1.0
|
FE2
|
B:SF4613
|
2.8
|
59.2
|
1.0
|
CB
|
B:CYS556
|
3.6
|
61.7
|
1.0
|
N
|
B:CYS556
|
3.7
|
61.9
|
1.0
|
S3
|
B:SF4613
|
3.9
|
59.0
|
1.0
|
CD
|
B:PRO529
|
3.9
|
59.0
|
1.0
|
CG
|
B:PRO529
|
3.9
|
59.5
|
1.0
|
N
|
B:LYS557
|
3.9
|
60.0
|
1.0
|
CA
|
B:CYS556
|
4.0
|
61.5
|
1.0
|
N
|
B:THR558
|
4.2
|
56.6
|
1.0
|
C
|
B:CYS556
|
4.3
|
60.2
|
1.0
|
CB
|
B:THR558
|
4.4
|
54.4
|
1.0
|
OG1
|
B:THR558
|
4.6
|
54.3
|
1.0
|
SG
|
B:CYS559
|
4.7
|
52.2
|
1.0
|
SG
|
B:CYS528
|
4.7
|
53.4
|
1.0
|
N
|
B:CYS559
|
4.8
|
55.9
|
1.0
|
C
|
B:HIS555
|
4.8
|
62.6
|
1.0
|
CG2
|
B:VAL554
|
4.8
|
66.5
|
1.0
|
N
|
B:HIS555
|
4.8
|
64.4
|
1.0
|
CA
|
B:THR558
|
4.9
|
55.8
|
1.0
|
CA
|
B:LYS557
|
4.9
|
58.7
|
1.0
|
N
|
B:VAL554
|
4.9
|
66.4
|
1.0
|
SG
|
B:CYS553
|
4.9
|
69.5
|
1.0
|
C
|
B:LYS557
|
5.0
|
57.5
|
1.0
|
|
Iron binding site 8 out
of 8 in 2gmh
Go back to
Iron Binding Sites List in 2gmh
Iron binding site 8 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase in Complexed with Ubiquinone within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe613
b:59.3
occ:1.00
|
FE4
|
B:SF4613
|
0.0
|
59.3
|
1.0
|
S1
|
B:SF4613
|
2.2
|
56.0
|
1.0
|
S2
|
B:SF4613
|
2.2
|
57.4
|
1.0
|
S3
|
B:SF4613
|
2.2
|
59.0
|
1.0
|
SG
|
B:CYS559
|
2.3
|
52.2
|
1.0
|
FE3
|
B:SF4613
|
2.7
|
59.8
|
1.0
|
FE1
|
B:SF4613
|
2.7
|
59.8
|
1.0
|
FE2
|
B:SF4613
|
2.7
|
59.2
|
1.0
|
CB
|
B:CYS559
|
3.4
|
54.2
|
1.0
|
S4
|
B:SF4613
|
3.8
|
58.4
|
1.0
|
N
|
B:CYS559
|
3.9
|
55.9
|
1.0
|
OH
|
B:TYR533
|
4.1
|
68.8
|
1.0
|
CD1
|
B:LEU504
|
4.2
|
66.5
|
1.0
|
CA
|
B:CYS559
|
4.3
|
54.8
|
1.0
|
CE1
|
B:TYR533
|
4.5
|
69.8
|
1.0
|
CD1
|
B:TRP570
|
4.6
|
54.4
|
1.0
|
N
|
B:THR558
|
4.7
|
56.6
|
1.0
|
SG
|
B:CYS556
|
4.7
|
66.8
|
1.0
|
SG
|
B:CYS528
|
4.8
|
53.4
|
1.0
|
SG
|
B:CYS553
|
4.8
|
69.5
|
1.0
|
CZ
|
B:TYR533
|
4.8
|
69.4
|
1.0
|
N
|
B:LYS557
|
4.9
|
60.0
|
1.0
|
|
Reference:
J.Zhang,
F.E.Frerman,
J.J.Kim.
Structure of Electron Transfer Flavoprotein-Ubiquinone Oxidoreductase and Electron Transfer to the Mitochondrial Ubiquinone Pool. Proc.Natl.Acad.Sci.Usa V. 103 16212 2006.
ISSN: ISSN 0027-8424
PubMed: 17050691
DOI: 10.1073/PNAS.0604567103
Page generated: Sat Aug 3 22:34:58 2024
|