Iron in PDB 2gmj: Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
Enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
All present enzymatic activity of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase:
1.5.5.1;
Protein crystallography data
The structure of Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase, PDB code: 2gmj
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)
|
28.75 /
2.60
|
Space group
|
P 4 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
154.839,
154.839,
130.199,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.8 /
25.5
|
Iron Binding Sites:
The binding sites of Iron atom in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
(pdb code 2gmj). 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, PDB code: 2gmj:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Iron binding site 1 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 1 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:8.7
occ:1.00
|
FE1
|
A:SF4610
|
0.0
|
8.7
|
1.0
|
S4
|
A:SF4610
|
2.3
|
7.1
|
1.0
|
S3
|
A:SF4610
|
2.3
|
6.7
|
1.0
|
S2
|
A:SF4610
|
2.3
|
8.0
|
1.0
|
SG
|
A:CYS559
|
2.7
|
12.4
|
1.0
|
FE2
|
A:SF4610
|
2.7
|
8.3
|
1.0
|
FE3
|
A:SF4610
|
2.7
|
6.8
|
1.0
|
FE4
|
A:SF4610
|
2.8
|
9.3
|
1.0
|
CB
|
A:CYS559
|
2.9
|
9.0
|
1.0
|
N
|
A:CYS559
|
3.6
|
11.7
|
1.0
|
S1
|
A:SF4610
|
3.8
|
10.1
|
1.0
|
CA
|
A:CYS559
|
3.9
|
11.4
|
1.0
|
CD1
|
A:LEU504
|
4.0
|
17.3
|
1.0
|
CE1
|
A:TYR533
|
4.4
|
10.4
|
1.0
|
OH
|
A:TYR533
|
4.4
|
9.6
|
1.0
|
N
|
A:THR558
|
4.6
|
9.7
|
1.0
|
C
|
A:THR558
|
4.8
|
11.8
|
1.0
|
CD1
|
A:TRP570
|
4.8
|
18.0
|
1.0
|
C
|
A:LYS557
|
4.8
|
10.0
|
1.0
|
CZ
|
A:TYR533
|
4.9
|
9.1
|
1.0
|
C
|
A:CYS559
|
4.9
|
11.8
|
1.0
|
N
|
A:LYS557
|
4.9
|
11.8
|
1.0
|
CG
|
A:LEU504
|
4.9
|
17.5
|
1.0
|
SG
|
A:CYS528
|
5.0
|
12.3
|
1.0
|
N
|
A:ASP560
|
5.0
|
12.8
|
1.0
|
SG
|
A:CYS556
|
5.0
|
14.9
|
1.0
|
|
Iron binding site 2 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 2 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:8.3
occ:1.00
|
FE2
|
A:SF4610
|
0.0
|
8.3
|
1.0
|
S3
|
A:SF4610
|
2.3
|
6.7
|
1.0
|
S4
|
A:SF4610
|
2.3
|
7.1
|
1.0
|
S1
|
A:SF4610
|
2.3
|
10.1
|
1.0
|
SG
|
A:CYS528
|
2.5
|
12.3
|
1.0
|
FE1
|
A:SF4610
|
2.7
|
8.7
|
1.0
|
FE3
|
A:SF4610
|
2.8
|
6.8
|
1.0
|
FE4
|
A:SF4610
|
2.9
|
9.3
|
1.0
|
CB
|
A:CYS528
|
3.4
|
15.0
|
1.0
|
S2
|
A:SF4610
|
3.9
|
8.0
|
1.0
|
CA
|
A:CYS528
|
4.1
|
14.5
|
1.0
|
CD
|
A:PRO529
|
4.2
|
15.1
|
1.0
|
CG2
|
A:VAL532
|
4.3
|
18.7
|
1.0
|
CB
|
A:VAL532
|
4.4
|
18.1
|
1.0
|
N
|
A:PRO529
|
4.5
|
14.8
|
1.0
|
C
|
A:CYS528
|
4.6
|
15.3
|
1.0
|
N
|
A:ALA530
|
4.7
|
15.7
|
1.0
|
CE1
|
A:TYR533
|
4.8
|
10.4
|
1.0
|
CB
|
A:ALA530
|
4.8
|
14.2
|
1.0
|
SG
|
A:CYS556
|
5.0
|
14.9
|
1.0
|
|
Iron binding site 3 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 3 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:6.8
occ:1.00
|
FE3
|
A:SF4610
|
0.0
|
6.8
|
1.0
|
S4
|
A:SF4610
|
2.2
|
7.1
|
1.0
|
S2
|
A:SF4610
|
2.3
|
8.0
|
1.0
|
S1
|
A:SF4610
|
2.3
|
10.1
|
1.0
|
SG
|
A:CYS553
|
2.5
|
16.2
|
1.0
|
FE1
|
A:SF4610
|
2.7
|
8.7
|
1.0
|
FE4
|
A:SF4610
|
2.8
|
9.3
|
1.0
|
FE2
|
A:SF4610
|
2.8
|
8.3
|
1.0
|
CB
|
A:CYS553
|
3.5
|
16.5
|
1.0
|
S3
|
A:SF4610
|
3.8
|
6.7
|
1.0
|
CA
|
A:CYS553
|
3.9
|
14.3
|
1.0
|
CD1
|
A:LEU504
|
4.1
|
17.3
|
1.0
|
N
|
A:HIS555
|
4.2
|
9.6
|
1.0
|
N
|
A:VAL554
|
4.2
|
12.1
|
1.0
|
NE1
|
A:TRP570
|
4.2
|
17.8
|
1.0
|
CD1
|
A:TRP570
|
4.4
|
18.0
|
1.0
|
C
|
A:CYS553
|
4.4
|
13.5
|
1.0
|
CA
|
A:HIS555
|
4.6
|
10.2
|
1.0
|
N
|
A:CYS556
|
4.6
|
12.1
|
1.0
|
CG
|
A:LEU504
|
4.7
|
17.5
|
1.0
|
CD2
|
A:LEU504
|
4.8
|
18.1
|
1.0
|
CG2
|
A:VAL532
|
4.9
|
18.7
|
1.0
|
SG
|
A:CYS559
|
5.0
|
12.4
|
1.0
|
|
Iron binding site 4 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 4 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe610
b:9.3
occ:1.00
|
FE4
|
A:SF4610
|
0.0
|
9.3
|
1.0
|
S2
|
A:SF4610
|
2.2
|
8.0
|
1.0
|
S3
|
A:SF4610
|
2.2
|
6.7
|
1.0
|
S1
|
A:SF4610
|
2.2
|
10.1
|
1.0
|
SG
|
A:CYS556
|
2.5
|
14.9
|
1.0
|
FE3
|
A:SF4610
|
2.8
|
6.8
|
1.0
|
FE1
|
A:SF4610
|
2.8
|
8.7
|
1.0
|
FE2
|
A:SF4610
|
2.9
|
8.3
|
1.0
|
N
|
A:CYS556
|
3.5
|
12.1
|
1.0
|
N
|
A:LYS557
|
3.6
|
11.8
|
1.0
|
CB
|
A:CYS556
|
3.7
|
14.7
|
1.0
|
S4
|
A:SF4610
|
3.9
|
7.1
|
1.0
|
N
|
A:THR558
|
3.9
|
9.7
|
1.0
|
CA
|
A:CYS556
|
3.9
|
13.1
|
1.0
|
C
|
A:CYS556
|
4.1
|
13.3
|
1.0
|
CD
|
A:PRO529
|
4.2
|
15.1
|
1.0
|
CA
|
A:LYS557
|
4.4
|
10.0
|
1.0
|
CB
|
A:THR558
|
4.5
|
10.2
|
1.0
|
C
|
A:LYS557
|
4.5
|
10.0
|
1.0
|
N
|
A:CYS559
|
4.6
|
11.7
|
1.0
|
C
|
A:HIS555
|
4.6
|
11.5
|
1.0
|
CG
|
A:PRO529
|
4.6
|
15.4
|
1.0
|
OG1
|
A:THR558
|
4.6
|
11.5
|
1.0
|
CA
|
A:THR558
|
4.7
|
11.1
|
1.0
|
N
|
A:HIS555
|
4.9
|
9.6
|
1.0
|
SG
|
A:CYS553
|
4.9
|
16.2
|
1.0
|
CG2
|
A:VAL554
|
4.9
|
5.4
|
1.0
|
SG
|
A:CYS528
|
4.9
|
12.3
|
1.0
|
CA
|
A:HIS555
|
5.0
|
10.2
|
1.0
|
|
Iron binding site 5 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 5 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe612
b:51.5
occ:1.00
|
FE1
|
B:SF4612
|
0.0
|
51.5
|
1.0
|
S4
|
B:SF4612
|
2.3
|
53.6
|
1.0
|
S3
|
B:SF4612
|
2.3
|
54.3
|
1.0
|
S2
|
B:SF4612
|
2.3
|
54.8
|
1.0
|
SG
|
B:CYS559
|
2.4
|
65.3
|
1.0
|
FE4
|
B:SF4612
|
2.7
|
53.7
|
1.0
|
FE2
|
B:SF4612
|
2.8
|
53.7
|
1.0
|
FE3
|
B:SF4612
|
2.8
|
54.0
|
1.0
|
CB
|
B:CYS559
|
3.3
|
60.1
|
1.0
|
S1
|
B:SF4612
|
3.9
|
53.2
|
1.0
|
N
|
B:CYS559
|
4.0
|
59.4
|
1.0
|
CE1
|
B:TYR533
|
4.3
|
62.9
|
1.0
|
CA
|
B:CYS559
|
4.3
|
59.1
|
1.0
|
OH
|
B:TYR533
|
4.4
|
62.8
|
1.0
|
CD2
|
B:LEU504
|
4.5
|
62.0
|
1.0
|
SG
|
B:CYS528
|
4.6
|
54.1
|
1.0
|
SG
|
B:CYS553
|
4.7
|
63.4
|
1.0
|
CG
|
B:LEU504
|
4.8
|
61.6
|
1.0
|
N
|
B:THR558
|
4.8
|
58.7
|
1.0
|
CD1
|
B:LEU504
|
4.8
|
61.7
|
1.0
|
CZ
|
B:TYR533
|
4.8
|
62.9
|
1.0
|
CD1
|
B:TRP570
|
4.9
|
60.1
|
1.0
|
SG
|
B:CYS556
|
5.0
|
63.4
|
1.0
|
|
Iron binding site 6 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 6 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe612
b:53.7
occ:1.00
|
FE2
|
B:SF4612
|
0.0
|
53.7
|
1.0
|
S3
|
B:SF4612
|
2.3
|
54.3
|
1.0
|
S4
|
B:SF4612
|
2.3
|
53.6
|
1.0
|
S1
|
B:SF4612
|
2.4
|
53.2
|
1.0
|
SG
|
B:CYS528
|
2.4
|
54.1
|
1.0
|
FE4
|
B:SF4612
|
2.8
|
53.7
|
1.0
|
FE1
|
B:SF4612
|
2.8
|
51.5
|
1.0
|
FE3
|
B:SF4612
|
2.9
|
54.0
|
1.0
|
CB
|
B:CYS528
|
3.7
|
58.4
|
1.0
|
S2
|
B:SF4612
|
3.9
|
54.8
|
1.0
|
CA
|
B:CYS528
|
3.9
|
58.5
|
1.0
|
CD
|
B:PRO529
|
4.0
|
58.9
|
1.0
|
CG2
|
B:VAL532
|
4.1
|
64.7
|
1.0
|
CB
|
B:VAL532
|
4.2
|
64.7
|
1.0
|
N
|
B:PRO529
|
4.3
|
59.6
|
1.0
|
C
|
B:CYS528
|
4.4
|
59.2
|
1.0
|
N
|
B:ALA530
|
4.4
|
60.8
|
1.0
|
CB
|
B:ALA530
|
4.6
|
61.2
|
1.0
|
CG
|
B:PRO529
|
4.6
|
58.7
|
1.0
|
CE1
|
B:TYR533
|
4.6
|
62.9
|
1.0
|
CA
|
B:CYS553
|
4.7
|
63.5
|
1.0
|
SG
|
B:CYS556
|
4.9
|
63.4
|
1.0
|
CA
|
B:ALA530
|
4.9
|
61.2
|
1.0
|
CG1
|
B:VAL532
|
5.0
|
65.0
|
1.0
|
SG
|
B:CYS559
|
5.0
|
65.3
|
1.0
|
|
Iron binding site 7 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 7 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe612
b:54.0
occ:1.00
|
FE3
|
B:SF4612
|
0.0
|
54.0
|
1.0
|
S4
|
B:SF4612
|
2.2
|
53.6
|
1.0
|
S2
|
B:SF4612
|
2.3
|
54.8
|
1.0
|
S1
|
B:SF4612
|
2.3
|
53.2
|
1.0
|
SG
|
B:CYS553
|
2.5
|
63.4
|
1.0
|
FE4
|
B:SF4612
|
2.7
|
53.7
|
1.0
|
FE1
|
B:SF4612
|
2.8
|
51.5
|
1.0
|
FE2
|
B:SF4612
|
2.9
|
53.7
|
1.0
|
CB
|
B:CYS553
|
3.2
|
63.3
|
1.0
|
CA
|
B:CYS553
|
3.3
|
63.5
|
1.0
|
N
|
B:VAL554
|
3.6
|
63.9
|
1.0
|
C
|
B:CYS553
|
3.9
|
63.6
|
1.0
|
N
|
B:HIS555
|
3.9
|
64.0
|
1.0
|
S3
|
B:SF4612
|
3.9
|
54.3
|
1.0
|
N
|
B:CYS556
|
4.4
|
62.2
|
1.0
|
CA
|
B:HIS555
|
4.5
|
64.2
|
1.0
|
NE1
|
B:TRP570
|
4.6
|
60.5
|
1.0
|
N
|
B:CYS553
|
4.6
|
64.3
|
1.0
|
C
|
B:VAL554
|
4.7
|
63.6
|
1.0
|
CA
|
B:VAL554
|
4.7
|
63.5
|
1.0
|
CD1
|
B:TRP570
|
4.8
|
60.1
|
1.0
|
CG2
|
B:VAL532
|
4.8
|
64.7
|
1.0
|
SG
|
B:CYS556
|
4.8
|
63.4
|
1.0
|
SG
|
B:CYS559
|
4.9
|
65.3
|
1.0
|
CD1
|
B:LEU504
|
4.9
|
61.7
|
1.0
|
O
|
B:CYS553
|
4.9
|
62.9
|
1.0
|
C
|
B:HIS555
|
5.0
|
63.4
|
1.0
|
CD2
|
B:LEU504
|
5.0
|
62.0
|
1.0
|
|
Iron binding site 8 out
of 8 in 2gmj
Go back to
Iron Binding Sites List in 2gmj
Iron binding site 8 out
of 8 in the Structure of Porcine Electron Transfer Flavoprotein- Ubiquinone Oxidoreductase
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 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe612
b:53.7
occ:1.00
|
FE4
|
B:SF4612
|
0.0
|
53.7
|
1.0
|
S1
|
B:SF4612
|
2.2
|
53.2
|
1.0
|
S2
|
B:SF4612
|
2.2
|
54.8
|
1.0
|
S3
|
B:SF4612
|
2.2
|
54.3
|
1.0
|
SG
|
B:CYS556
|
2.4
|
63.4
|
1.0
|
FE3
|
B:SF4612
|
2.7
|
54.0
|
1.0
|
FE1
|
B:SF4612
|
2.7
|
51.5
|
1.0
|
FE2
|
B:SF4612
|
2.8
|
53.7
|
1.0
|
S4
|
B:SF4612
|
3.8
|
53.6
|
1.0
|
N
|
B:CYS556
|
3.8
|
62.2
|
1.0
|
CB
|
B:CYS556
|
3.8
|
61.8
|
1.0
|
N
|
B:LYS557
|
3.9
|
60.1
|
1.0
|
CD
|
B:PRO529
|
4.0
|
58.9
|
1.0
|
N
|
B:THR558
|
4.1
|
58.7
|
1.0
|
CG
|
B:PRO529
|
4.1
|
58.7
|
1.0
|
CA
|
B:CYS556
|
4.1
|
61.3
|
1.0
|
C
|
B:CYS556
|
4.4
|
60.5
|
1.0
|
CB
|
B:THR558
|
4.5
|
59.5
|
1.0
|
SG
|
B:CYS559
|
4.6
|
65.3
|
1.0
|
N
|
B:CYS559
|
4.7
|
59.4
|
1.0
|
CG2
|
B:VAL554
|
4.8
|
62.5
|
1.0
|
CA
|
B:THR558
|
4.8
|
59.1
|
1.0
|
CA
|
B:LYS557
|
4.8
|
59.3
|
1.0
|
OG1
|
B:THR558
|
4.9
|
60.4
|
1.0
|
C
|
B:HIS555
|
4.9
|
63.4
|
1.0
|
SG
|
B:CYS528
|
4.9
|
54.1
|
1.0
|
N
|
B:HIS555
|
4.9
|
64.0
|
1.0
|
C
|
B:LYS557
|
4.9
|
59.2
|
1.0
|
N
|
B:VAL554
|
5.0
|
63.9
|
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 22:35:24 2024
|