Iron in PDB 3iq5: Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
Protein crystallography data
The structure of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination, PDB code: 3iq5
was solved by
J.N.Brodin,
F.A.Tezcan,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
50.00 /
2.05
|
Space group
|
I 41
|
Cell size a, b, c (Å), α, β, γ (°)
|
69.153,
69.153,
186.935,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.9 /
27.7
|
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
(pdb code 3iq5). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination, PDB code: 3iq5:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 3iq5
Go back to
Iron Binding Sites List in 3iq5
Iron binding site 1 out
of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe150
b:17.8
occ:1.00
|
FE
|
A:HEM150
|
0.0
|
17.8
|
1.0
|
ND
|
A:HEM150
|
1.9
|
17.1
|
1.0
|
NB
|
A:HEM150
|
2.0
|
16.9
|
1.0
|
NC
|
A:HEM150
|
2.0
|
17.7
|
1.0
|
NA
|
A:HEM150
|
2.1
|
18.3
|
1.0
|
NE2
|
A:HIS102
|
2.1
|
14.3
|
1.0
|
SD
|
A:MET7
|
2.2
|
19.6
|
1.0
|
C4B
|
A:HEM150
|
3.0
|
20.8
|
1.0
|
C1C
|
A:HEM150
|
3.0
|
18.9
|
1.0
|
C1D
|
A:HEM150
|
3.0
|
18.8
|
1.0
|
C4D
|
A:HEM150
|
3.0
|
21.9
|
1.0
|
CD2
|
A:HIS102
|
3.0
|
19.0
|
1.0
|
C1A
|
A:HEM150
|
3.1
|
19.2
|
1.0
|
C4C
|
A:HEM150
|
3.1
|
18.2
|
1.0
|
C1B
|
A:HEM150
|
3.1
|
16.8
|
1.0
|
CE1
|
A:HIS102
|
3.1
|
19.1
|
1.0
|
C4A
|
A:HEM150
|
3.1
|
18.1
|
1.0
|
CHC
|
A:HEM150
|
3.3
|
16.6
|
1.0
|
CE
|
A:MET7
|
3.3
|
18.1
|
1.0
|
CG
|
A:MET7
|
3.4
|
17.0
|
1.0
|
CHD
|
A:HEM150
|
3.4
|
13.4
|
1.0
|
CHA
|
A:HEM150
|
3.4
|
18.9
|
1.0
|
CHB
|
A:HEM150
|
3.5
|
14.6
|
1.0
|
CG
|
A:HIS102
|
4.2
|
20.2
|
1.0
|
ND1
|
A:HIS102
|
4.2
|
18.0
|
1.0
|
CB
|
A:MET7
|
4.2
|
18.6
|
1.0
|
C2D
|
A:HEM150
|
4.2
|
16.7
|
1.0
|
C3B
|
A:HEM150
|
4.3
|
19.3
|
1.0
|
C2B
|
A:HEM150
|
4.3
|
13.9
|
1.0
|
C3D
|
A:HEM150
|
4.3
|
20.9
|
1.0
|
C2C
|
A:HEM150
|
4.3
|
16.9
|
1.0
|
C2A
|
A:HEM150
|
4.3
|
18.3
|
1.0
|
C3A
|
A:HEM150
|
4.4
|
19.4
|
1.0
|
C3C
|
A:HEM150
|
4.4
|
19.4
|
1.0
|
|
Iron binding site 2 out
of 4 in 3iq5
Go back to
Iron Binding Sites List in 3iq5
Iron binding site 2 out
of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe150
b:19.0
occ:1.00
|
FE
|
B:HEM150
|
0.0
|
19.0
|
1.0
|
ND
|
B:HEM150
|
1.9
|
14.3
|
1.0
|
NA
|
B:HEM150
|
2.0
|
21.0
|
1.0
|
NB
|
B:HEM150
|
2.0
|
19.5
|
1.0
|
NC
|
B:HEM150
|
2.1
|
17.9
|
1.0
|
NE2
|
B:HIS102
|
2.1
|
18.4
|
1.0
|
SD
|
B:MET7
|
2.3
|
22.0
|
1.0
|
C4D
|
B:HEM150
|
3.0
|
20.3
|
1.0
|
C1A
|
B:HEM150
|
3.0
|
25.6
|
1.0
|
C1D
|
B:HEM150
|
3.0
|
18.4
|
1.0
|
CD2
|
B:HIS102
|
3.0
|
20.5
|
1.0
|
C4B
|
B:HEM150
|
3.0
|
19.2
|
1.0
|
C1C
|
B:HEM150
|
3.1
|
16.5
|
1.0
|
C1B
|
B:HEM150
|
3.1
|
24.1
|
1.0
|
CE1
|
B:HIS102
|
3.1
|
20.7
|
1.0
|
C4A
|
B:HEM150
|
3.1
|
24.4
|
1.0
|
C4C
|
B:HEM150
|
3.1
|
17.7
|
1.0
|
CE
|
B:MET7
|
3.3
|
18.0
|
1.0
|
CHA
|
B:HEM150
|
3.4
|
16.2
|
1.0
|
CHC
|
B:HEM150
|
3.4
|
15.9
|
1.0
|
CG
|
B:MET7
|
3.4
|
19.1
|
1.0
|
CHD
|
B:HEM150
|
3.4
|
17.6
|
1.0
|
CHB
|
B:HEM150
|
3.5
|
18.0
|
1.0
|
ND1
|
B:HIS102
|
4.2
|
16.9
|
1.0
|
CG
|
B:HIS102
|
4.2
|
21.0
|
1.0
|
CB
|
B:MET7
|
4.2
|
17.6
|
1.0
|
C3D
|
B:HEM150
|
4.3
|
19.4
|
1.0
|
C2D
|
B:HEM150
|
4.3
|
21.5
|
1.0
|
C2A
|
B:HEM150
|
4.3
|
26.8
|
1.0
|
C2B
|
B:HEM150
|
4.3
|
20.4
|
1.0
|
C3B
|
B:HEM150
|
4.3
|
21.1
|
1.0
|
C3A
|
B:HEM150
|
4.3
|
24.9
|
1.0
|
C2C
|
B:HEM150
|
4.4
|
14.3
|
1.0
|
C3C
|
B:HEM150
|
4.4
|
21.4
|
1.0
|
NH1
|
B:ARG106
|
4.9
|
41.1
|
1.0
|
CA
|
B:MET7
|
5.0
|
20.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 3iq5
Go back to
Iron Binding Sites List in 3iq5
Iron binding site 3 out
of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe150
b:33.7
occ:1.00
|
FE
|
C:HEM150
|
0.0
|
33.7
|
1.0
|
NE2
|
C:HIS102
|
1.9
|
21.1
|
1.0
|
NA
|
C:HEM150
|
2.0
|
35.6
|
1.0
|
NB
|
C:HEM150
|
2.0
|
29.9
|
1.0
|
ND
|
C:HEM150
|
2.0
|
32.9
|
1.0
|
NC
|
C:HEM150
|
2.1
|
30.2
|
1.0
|
SD
|
C:MET7
|
2.2
|
33.3
|
1.0
|
CE1
|
C:HIS102
|
2.8
|
28.0
|
1.0
|
C4B
|
C:HEM150
|
3.0
|
33.3
|
1.0
|
CD2
|
C:HIS102
|
3.0
|
27.0
|
1.0
|
C1A
|
C:HEM150
|
3.0
|
36.7
|
1.0
|
C4D
|
C:HEM150
|
3.0
|
35.2
|
1.0
|
C1C
|
C:HEM150
|
3.0
|
29.7
|
1.0
|
C4A
|
C:HEM150
|
3.0
|
35.9
|
1.0
|
C1B
|
C:HEM150
|
3.1
|
34.3
|
1.0
|
C1D
|
C:HEM150
|
3.2
|
33.1
|
1.0
|
C4C
|
C:HEM150
|
3.2
|
29.1
|
1.0
|
CHC
|
C:HEM150
|
3.3
|
28.1
|
1.0
|
CHA
|
C:HEM150
|
3.3
|
33.8
|
1.0
|
CHB
|
C:HEM150
|
3.4
|
33.2
|
1.0
|
CG
|
C:MET7
|
3.5
|
37.9
|
1.0
|
CE
|
C:MET7
|
3.5
|
30.9
|
1.0
|
CHD
|
C:HEM150
|
3.6
|
30.7
|
1.0
|
ND1
|
C:HIS102
|
3.9
|
28.2
|
1.0
|
CG
|
C:HIS102
|
4.1
|
26.4
|
1.0
|
CB
|
C:MET7
|
4.2
|
35.5
|
1.0
|
C3B
|
C:HEM150
|
4.3
|
34.4
|
1.0
|
C3A
|
C:HEM150
|
4.3
|
39.5
|
1.0
|
C2B
|
C:HEM150
|
4.3
|
32.0
|
1.0
|
C2A
|
C:HEM150
|
4.3
|
36.7
|
1.0
|
C3D
|
C:HEM150
|
4.3
|
36.1
|
1.0
|
C2C
|
C:HEM150
|
4.4
|
24.7
|
1.0
|
C2D
|
C:HEM150
|
4.4
|
34.4
|
1.0
|
C3C
|
C:HEM150
|
4.4
|
27.9
|
1.0
|
CA
|
C:MET7
|
4.9
|
40.1
|
1.0
|
|
Iron binding site 4 out
of 4 in 3iq5
Go back to
Iron Binding Sites List in 3iq5
Iron binding site 4 out
of 4 in the Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of An Engineered Metal-Free Tetrameric Cytochrome CB562 Complex Templated By Zn-Coordination within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe150
b:38.2
occ:1.00
|
FE
|
D:HEM150
|
0.0
|
38.2
|
1.0
|
NB
|
D:HEM150
|
1.9
|
34.7
|
1.0
|
NE2
|
D:HIS102
|
1.9
|
27.0
|
1.0
|
NC
|
D:HEM150
|
2.0
|
32.2
|
1.0
|
ND
|
D:HEM150
|
2.1
|
38.6
|
1.0
|
NA
|
D:HEM150
|
2.1
|
40.9
|
1.0
|
SD
|
D:MET7
|
2.3
|
44.5
|
1.0
|
CE1
|
D:HIS102
|
2.9
|
31.4
|
1.0
|
C4B
|
D:HEM150
|
2.9
|
37.5
|
1.0
|
CD2
|
D:HIS102
|
2.9
|
31.9
|
1.0
|
C1C
|
D:HEM150
|
3.0
|
34.9
|
1.0
|
C1B
|
D:HEM150
|
3.0
|
40.6
|
1.0
|
C4A
|
D:HEM150
|
3.1
|
41.7
|
1.0
|
C4C
|
D:HEM150
|
3.1
|
34.4
|
1.0
|
C1D
|
D:HEM150
|
3.1
|
40.7
|
1.0
|
C4D
|
D:HEM150
|
3.1
|
41.4
|
1.0
|
C1A
|
D:HEM150
|
3.1
|
41.8
|
1.0
|
CHC
|
D:HEM150
|
3.3
|
34.4
|
1.0
|
CE
|
D:MET7
|
3.3
|
42.1
|
1.0
|
CHB
|
D:HEM150
|
3.4
|
40.5
|
1.0
|
CHD
|
D:HEM150
|
3.5
|
34.4
|
1.0
|
CHA
|
D:HEM150
|
3.5
|
40.2
|
1.0
|
CG
|
D:MET7
|
3.6
|
41.5
|
1.0
|
ND1
|
D:HIS102
|
4.0
|
29.4
|
1.0
|
CG
|
D:HIS102
|
4.0
|
35.1
|
1.0
|
C3B
|
D:HEM150
|
4.2
|
35.4
|
1.0
|
C2B
|
D:HEM150
|
4.2
|
37.1
|
1.0
|
C2C
|
D:HEM150
|
4.3
|
33.0
|
1.0
|
C3A
|
D:HEM150
|
4.3
|
43.0
|
1.0
|
C3C
|
D:HEM150
|
4.4
|
31.5
|
1.0
|
C2D
|
D:HEM150
|
4.4
|
40.6
|
1.0
|
C3D
|
D:HEM150
|
4.4
|
43.6
|
1.0
|
C2A
|
D:HEM150
|
4.4
|
46.5
|
1.0
|
CB
|
D:MET7
|
4.5
|
41.4
|
1.0
|
|
Reference:
J.D.Brodin,
A.Medina-Morales,
T.Ni,
E.N.Salgado,
X.I.Ambroggio,
F.A.Tezcan.
Evolution of Metal Selectivity in Templated Protein Interfaces. J.Am.Chem.Soc. V. 132 8610 2010.
ISSN: ISSN 0002-7863
PubMed: 20515031
DOI: 10.1021/JA910844N
Page generated: Sun Aug 4 12:18:16 2024
|