Iron in PDB 1eue: Rat Outer Mitochondrial Membrane Cytochrome B5
Protein crystallography data
The structure of Rat Outer Mitochondrial Membrane Cytochrome B5, PDB code: 1eue
was solved by
V.Oganesyan,
X.Zhang,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
11.93 /
1.80
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
46.230,
70.770,
72.440,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.7 /
23.2
|
Iron Binding Sites:
The binding sites of Iron atom in the Rat Outer Mitochondrial Membrane Cytochrome B5
(pdb code 1eue). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the
Rat Outer Mitochondrial Membrane Cytochrome B5, PDB code: 1eue:
Jump to Iron binding site number:
1;
2;
Iron binding site 1 out
of 2 in 1eue
Go back to
Iron Binding Sites List in 1eue
Iron binding site 1 out
of 2 in the Rat Outer Mitochondrial Membrane Cytochrome B5
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Rat Outer Mitochondrial Membrane Cytochrome B5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe201
b:27.0
occ:1.00
|
FE
|
A:HEM201
|
0.0
|
27.0
|
1.0
|
NB
|
A:HEM201
|
2.0
|
23.8
|
1.0
|
ND
|
A:HEM201
|
2.0
|
28.2
|
1.0
|
NC
|
A:HEM201
|
2.0
|
25.7
|
1.0
|
NA
|
A:HEM201
|
2.0
|
27.8
|
1.0
|
NE2
|
A:HIS39
|
2.1
|
25.2
|
1.0
|
NE2
|
A:HIS63
|
2.2
|
24.3
|
1.0
|
C1B
|
A:HEM201
|
3.0
|
25.0
|
1.0
|
CD2
|
A:HIS63
|
3.0
|
27.6
|
1.0
|
C1D
|
A:HEM201
|
3.0
|
28.0
|
1.0
|
C4A
|
A:HEM201
|
3.0
|
27.1
|
1.0
|
C4B
|
A:HEM201
|
3.0
|
25.8
|
1.0
|
C4C
|
A:HEM201
|
3.0
|
25.6
|
1.0
|
C4D
|
A:HEM201
|
3.1
|
30.3
|
1.0
|
C1A
|
A:HEM201
|
3.1
|
28.3
|
1.0
|
CD2
|
A:HIS39
|
3.1
|
25.0
|
1.0
|
C1C
|
A:HEM201
|
3.1
|
25.4
|
1.0
|
CE1
|
A:HIS39
|
3.1
|
26.4
|
1.0
|
CE1
|
A:HIS63
|
3.3
|
28.8
|
1.0
|
CHD
|
A:HEM201
|
3.4
|
24.6
|
1.0
|
CHB
|
A:HEM201
|
3.4
|
26.3
|
1.0
|
CHC
|
A:HEM201
|
3.4
|
23.2
|
1.0
|
CHA
|
A:HEM201
|
3.4
|
28.1
|
1.0
|
ND1
|
A:HIS39
|
4.2
|
25.4
|
1.0
|
CG
|
A:HIS63
|
4.2
|
26.5
|
1.0
|
CG
|
A:HIS39
|
4.2
|
26.4
|
1.0
|
C2B
|
A:HEM201
|
4.2
|
26.3
|
1.0
|
C3A
|
A:HEM201
|
4.3
|
29.7
|
1.0
|
C2A
|
A:HEM201
|
4.3
|
30.6
|
1.0
|
C2D
|
A:HEM201
|
4.3
|
29.0
|
1.0
|
C3B
|
A:HEM201
|
4.3
|
26.7
|
1.0
|
C2C
|
A:HEM201
|
4.3
|
25.9
|
1.0
|
C3C
|
A:HEM201
|
4.3
|
27.1
|
1.0
|
C3D
|
A:HEM201
|
4.3
|
30.8
|
1.0
|
ND1
|
A:HIS63
|
4.3
|
24.1
|
1.0
|
N
|
A:GLY41
|
5.0
|
28.9
|
1.0
|
|
Iron binding site 2 out
of 2 in 1eue
Go back to
Iron Binding Sites List in 1eue
Iron binding site 2 out
of 2 in the Rat Outer Mitochondrial Membrane Cytochrome B5
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Rat Outer Mitochondrial Membrane Cytochrome B5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe201
b:36.4
occ:1.00
|
FE
|
B:HEM201
|
0.0
|
36.4
|
1.0
|
NB
|
B:HEM201
|
1.9
|
33.6
|
1.0
|
ND
|
B:HEM201
|
2.0
|
38.4
|
1.0
|
NA
|
B:HEM201
|
2.0
|
37.0
|
1.0
|
NC
|
B:HEM201
|
2.0
|
33.9
|
1.0
|
NE2
|
B:HIS63
|
2.1
|
31.3
|
1.0
|
NE2
|
B:HIS39
|
2.1
|
33.5
|
1.0
|
C1B
|
B:HEM201
|
3.0
|
34.8
|
1.0
|
C4A
|
B:HEM201
|
3.0
|
36.8
|
1.0
|
C1D
|
B:HEM201
|
3.0
|
39.1
|
1.0
|
C4B
|
B:HEM201
|
3.0
|
32.9
|
1.0
|
CD2
|
B:HIS63
|
3.1
|
31.4
|
1.0
|
CD2
|
B:HIS39
|
3.1
|
32.6
|
1.0
|
CE1
|
B:HIS63
|
3.1
|
30.3
|
1.0
|
C1A
|
B:HEM201
|
3.1
|
39.5
|
1.0
|
C4D
|
B:HEM201
|
3.1
|
39.9
|
1.0
|
C4C
|
B:HEM201
|
3.1
|
34.2
|
1.0
|
C1C
|
B:HEM201
|
3.1
|
32.2
|
1.0
|
CE1
|
B:HIS39
|
3.2
|
31.9
|
1.0
|
CHB
|
B:HEM201
|
3.4
|
35.4
|
1.0
|
CHD
|
B:HEM201
|
3.4
|
36.4
|
1.0
|
CHC
|
B:HEM201
|
3.5
|
30.8
|
1.0
|
CHA
|
B:HEM201
|
3.5
|
39.9
|
1.0
|
ND1
|
B:HIS63
|
4.2
|
32.1
|
1.0
|
CG
|
B:HIS63
|
4.2
|
32.4
|
1.0
|
C2B
|
B:HEM201
|
4.2
|
34.8
|
1.0
|
C3A
|
B:HEM201
|
4.2
|
39.1
|
1.0
|
CG
|
B:HIS39
|
4.2
|
33.6
|
1.0
|
C2A
|
B:HEM201
|
4.2
|
41.4
|
1.0
|
ND1
|
B:HIS39
|
4.3
|
32.5
|
1.0
|
C2D
|
B:HEM201
|
4.3
|
40.4
|
1.0
|
C3B
|
B:HEM201
|
4.3
|
34.3
|
1.0
|
C3C
|
B:HEM201
|
4.3
|
35.2
|
1.0
|
C2C
|
B:HEM201
|
4.3
|
33.8
|
1.0
|
C3D
|
B:HEM201
|
4.3
|
41.7
|
1.0
|
CD1
|
B:ILE61
|
4.9
|
48.0
|
1.0
|
|
Reference:
M.Wirtz,
V.Oganesyan,
X.Zhang,
J.Studer,
M.Rivera.
Modulation of Redox Potential in Electron Transfer Proteins: Effects of Complex Formation on the Active Site Microenvironment of Cytochrome B5. Faraday Disc.Chem.Soc V. 116 221 2001.
ISSN: ISSN 1359-6640
PubMed: 11197480
Page generated: Sat Aug 3 04:37:53 2024
|