Iron in PDB 9cqx: Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
Enzymatic activity of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
All present enzymatic activity of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon:
1.18.6.1;
Other elements in 9cqx:
The structure of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon also contains other interesting chemical elements:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
20;
Page 3, Binding sites: 21 -
30;
Page 4, Binding sites: 31 -
32;
Binding sites:
The binding sites of Iron atom in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
(pdb code 9cqx). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 32 binding sites of Iron where determined in the
Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon, PDB code: 9cqx:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 32 in 9cqx
Go back to
Iron Binding Sites List in 9cqx
Iron binding site 1 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:52.3
occ:1.00
|
FE1
|
A:ICS502
|
0.0
|
52.3
|
1.0
|
S2A
|
A:ICS502
|
2.3
|
36.2
|
1.0
|
SG
|
A:CYS275
|
2.3
|
39.7
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
39.8
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
40.2
|
1.0
|
FE4
|
A:ICS502
|
2.7
|
47.4
|
1.0
|
FE3
|
A:ICS502
|
2.7
|
51.0
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
45.8
|
1.0
|
CB
|
A:CYS275
|
3.4
|
33.6
|
1.0
|
CX
|
A:ICS502
|
3.4
|
47.0
|
1.0
|
CB
|
A:LEU358
|
4.1
|
38.7
|
1.0
|
OG
|
A:SER278
|
4.2
|
43.8
|
1.0
|
CB
|
A:SER278
|
4.4
|
34.7
|
1.0
|
CA
|
A:CYS275
|
4.6
|
32.8
|
1.0
|
CE2
|
A:TYR229
|
4.7
|
34.6
|
1.0
|
N
|
A:LEU358
|
4.8
|
44.1
|
1.0
|
S2B
|
A:ICS502
|
4.8
|
40.3
|
1.0
|
S5A
|
A:ICS502
|
4.8
|
38.2
|
1.0
|
CD2
|
A:LEU358
|
4.8
|
37.5
|
1.0
|
S3A
|
A:ICS502
|
4.8
|
38.1
|
1.0
|
N
|
A:SER278
|
5.0
|
35.8
|
1.0
|
FE7
|
A:ICS502
|
5.0
|
47.5
|
1.0
|
FE6
|
A:ICS502
|
5.0
|
50.7
|
1.0
|
|
Iron binding site 2 out
of 32 in 9cqx
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Iron Binding Sites List in 9cqx
Iron binding site 2 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:45.8
occ:1.00
|
FE2
|
A:ICS502
|
0.0
|
45.8
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S2B
|
A:ICS502
|
2.2
|
40.3
|
1.0
|
S2A
|
A:ICS502
|
2.2
|
36.2
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
40.2
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
50.7
|
1.0
|
FE4
|
A:ICS502
|
2.7
|
47.4
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
52.3
|
1.0
|
FE3
|
A:ICS502
|
2.7
|
51.0
|
1.0
|
FE5
|
A:ICS502
|
3.7
|
54.2
|
1.0
|
FE7
|
A:ICS502
|
3.7
|
47.5
|
1.0
|
S4A
|
A:ICS502
|
3.9
|
39.8
|
1.0
|
CE1
|
A:HIS195
|
4.0
|
27.9
|
1.0
|
CZ
|
A:PHE381
|
4.1
|
39.5
|
1.0
|
NE2
|
A:HIS195
|
4.2
|
29.1
|
1.0
|
S3B
|
A:ICS502
|
4.2
|
40.0
|
1.0
|
S1B
|
A:ICS502
|
4.2
|
46.0
|
1.0
|
CE1
|
A:PHE381
|
4.4
|
36.0
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
38.1
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
38.2
|
1.0
|
CG1
|
A:VAL70
|
4.5
|
25.4
|
1.0
|
SG
|
A:CYS275
|
4.7
|
39.7
|
1.0
|
N
|
A:GLY357
|
4.9
|
36.2
|
1.0
|
CG2
|
A:VAL70
|
5.0
|
35.0
|
1.0
|
|
Iron binding site 3 out
of 32 in 9cqx
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Iron Binding Sites List in 9cqx
Iron binding site 3 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:51.0
occ:1.00
|
FE3
|
A:ICS502
|
0.0
|
51.0
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S5A
|
A:ICS502
|
2.2
|
38.2
|
1.0
|
S4A
|
A:ICS502
|
2.2
|
39.8
|
1.0
|
S2A
|
A:ICS502
|
2.3
|
36.2
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
47.5
|
1.0
|
FE4
|
A:ICS502
|
2.6
|
47.4
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
52.3
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
45.8
|
1.0
|
FE6
|
A:ICS502
|
3.7
|
50.7
|
1.0
|
FE5
|
A:ICS502
|
3.7
|
54.2
|
1.0
|
S1A
|
A:ICS502
|
3.9
|
40.2
|
1.0
|
NH2
|
A:ARG96
|
4.0
|
36.2
|
1.0
|
S3B
|
A:ICS502
|
4.2
|
40.0
|
1.0
|
S4B
|
A:ICS502
|
4.2
|
43.7
|
1.0
|
CD2
|
A:TYR229
|
4.3
|
38.8
|
1.0
|
O
|
A:HOH810
|
4.4
|
41.1
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
40.3
|
1.0
|
CE2
|
A:TYR229
|
4.5
|
34.6
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
38.1
|
1.0
|
SG
|
A:CYS275
|
4.7
|
39.7
|
1.0
|
NE
|
A:ARG359
|
4.8
|
36.8
|
1.0
|
O
|
A:HOH629
|
4.9
|
42.5
|
1.0
|
|
Iron binding site 4 out
of 32 in 9cqx
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Iron Binding Sites List in 9cqx
Iron binding site 4 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:47.4
occ:1.00
|
FE4
|
A:ICS502
|
0.0
|
47.4
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S3A
|
A:ICS502
|
2.2
|
38.1
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
39.8
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
40.2
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
54.2
|
1.0
|
FE3
|
A:ICS502
|
2.6
|
51.0
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
45.8
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
52.3
|
1.0
|
FE7
|
A:ICS502
|
3.7
|
47.5
|
1.0
|
FE6
|
A:ICS502
|
3.7
|
50.7
|
1.0
|
N
|
A:LEU358
|
3.8
|
44.1
|
1.0
|
S2A
|
A:ICS502
|
3.8
|
36.2
|
1.0
|
N
|
A:GLY357
|
3.9
|
36.2
|
1.0
|
CB
|
A:LEU358
|
4.1
|
38.7
|
1.0
|
S4B
|
A:ICS502
|
4.3
|
43.7
|
1.0
|
S1B
|
A:ICS502
|
4.3
|
46.0
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
38.2
|
1.0
|
CA
|
A:LEU358
|
4.5
|
41.6
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
40.3
|
1.0
|
CA
|
A:GLY357
|
4.5
|
37.3
|
1.0
|
N
|
A:ARG359
|
4.6
|
42.8
|
1.0
|
C
|
A:GLY357
|
4.6
|
45.0
|
1.0
|
SG
|
A:CYS275
|
4.7
|
39.7
|
1.0
|
CG
|
A:ARG359
|
4.7
|
36.2
|
1.0
|
CD
|
A:ARG359
|
4.8
|
40.3
|
1.0
|
NE
|
A:ARG359
|
4.8
|
36.8
|
1.0
|
C
|
A:GLY356
|
4.9
|
38.3
|
1.0
|
CA
|
A:GLY356
|
5.0
|
37.2
|
1.0
|
|
Iron binding site 5 out
of 32 in 9cqx
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Iron Binding Sites List in 9cqx
Iron binding site 5 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:54.2
occ:1.00
|
FE5
|
A:ICS502
|
0.0
|
54.2
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S4B
|
A:ICS502
|
2.2
|
43.7
|
1.0
|
S3A
|
A:ICS502
|
2.3
|
38.1
|
1.0
|
S1B
|
A:ICS502
|
2.3
|
46.0
|
1.0
|
FE4
|
A:ICS502
|
2.6
|
47.4
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
47.5
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
50.7
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
63.8
|
1.0
|
FE2
|
A:ICS502
|
3.7
|
45.8
|
1.0
|
FE3
|
A:ICS502
|
3.7
|
51.0
|
1.0
|
S3B
|
A:ICS502
|
3.9
|
40.0
|
1.0
|
N
|
A:GLY356
|
4.2
|
41.2
|
1.0
|
CG2
|
A:ILE355
|
4.2
|
38.1
|
1.0
|
ND1
|
A:HIS442
|
4.2
|
39.3
|
1.0
|
CA
|
A:GLY356
|
4.3
|
37.2
|
1.0
|
S1A
|
A:ICS502
|
4.3
|
40.2
|
1.0
|
S4A
|
A:ICS502
|
4.3
|
39.8
|
1.0
|
CD
|
A:ARG359
|
4.4
|
40.3
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
40.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
38.2
|
1.0
|
N
|
A:GLY357
|
4.6
|
36.2
|
1.0
|
NE
|
A:ARG359
|
4.7
|
36.8
|
1.0
|
CE1
|
A:HIS442
|
4.7
|
41.6
|
1.0
|
C
|
A:GLY356
|
5.0
|
38.3
|
1.0
|
|
Iron binding site 6 out
of 32 in 9cqx
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Iron Binding Sites List in 9cqx
Iron binding site 6 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:50.7
occ:1.00
|
FE6
|
A:ICS502
|
0.0
|
50.7
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S2B
|
A:ICS502
|
2.2
|
40.3
|
1.0
|
S3B
|
A:ICS502
|
2.2
|
40.0
|
1.0
|
S1B
|
A:ICS502
|
2.2
|
46.0
|
1.0
|
FE2
|
A:ICS502
|
2.6
|
45.8
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
47.5
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
54.2
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
63.8
|
1.0
|
FE3
|
A:ICS502
|
3.7
|
51.0
|
1.0
|
FE4
|
A:ICS502
|
3.7
|
47.4
|
1.0
|
S4B
|
A:ICS502
|
3.8
|
43.7
|
1.0
|
O7
|
A:HCA501
|
4.1
|
41.0
|
1.0
|
CZ
|
A:PHE381
|
4.2
|
39.5
|
1.0
|
S2A
|
A:ICS502
|
4.2
|
36.2
|
1.0
|
S1A
|
A:ICS502
|
4.3
|
40.2
|
1.0
|
O1
|
A:HCA501
|
4.4
|
41.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
38.2
|
1.0
|
CG2
|
A:VAL70
|
4.5
|
35.0
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
38.1
|
1.0
|
CE2
|
A:PHE381
|
4.8
|
35.0
|
1.0
|
O5
|
A:HCA501
|
4.8
|
40.6
|
1.0
|
FE1
|
A:ICS502
|
5.0
|
52.3
|
1.0
|
|
Iron binding site 7 out
of 32 in 9cqx
Go back to
Iron Binding Sites List in 9cqx
Iron binding site 7 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:47.5
occ:1.00
|
FE7
|
A:ICS502
|
0.0
|
47.5
|
1.0
|
CX
|
A:ICS502
|
2.0
|
47.0
|
1.0
|
S5A
|
A:ICS502
|
2.2
|
38.2
|
1.0
|
S4B
|
A:ICS502
|
2.2
|
43.7
|
1.0
|
S3B
|
A:ICS502
|
2.2
|
40.0
|
1.0
|
FE3
|
A:ICS502
|
2.6
|
51.0
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
50.7
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
54.2
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
63.8
|
1.0
|
FE2
|
A:ICS502
|
3.7
|
45.8
|
1.0
|
FE4
|
A:ICS502
|
3.7
|
47.4
|
1.0
|
S1B
|
A:ICS502
|
3.8
|
46.0
|
1.0
|
NH2
|
A:ARG96
|
4.0
|
36.2
|
1.0
|
O
|
A:HOH728
|
4.0
|
31.9
|
1.0
|
NE
|
A:ARG96
|
4.2
|
32.7
|
1.0
|
S2A
|
A:ICS502
|
4.3
|
36.2
|
1.0
|
S4A
|
A:ICS502
|
4.3
|
39.8
|
1.0
|
O5
|
A:HCA501
|
4.3
|
40.6
|
1.0
|
S2B
|
A:ICS502
|
4.4
|
40.3
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
38.1
|
1.0
|
CZ
|
A:ARG359
|
4.5
|
33.8
|
1.0
|
NH2
|
A:ARG359
|
4.6
|
32.7
|
1.0
|
CZ
|
A:ARG96
|
4.6
|
30.6
|
1.0
|
NE
|
A:ARG359
|
4.6
|
36.8
|
1.0
|
NH1
|
A:ARG359
|
4.9
|
39.6
|
1.0
|
FE1
|
A:ICS502
|
5.0
|
52.3
|
1.0
|
|
Iron binding site 8 out
of 32 in 9cqx
Go back to
Iron Binding Sites List in 9cqx
Iron binding site 8 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:68.5
occ:1.00
|
OE2
|
D:GLU109
|
2.1
|
60.6
|
1.0
|
OD2
|
B:ASP353
|
2.2
|
56.0
|
1.0
|
OD2
|
B:ASP357
|
2.3
|
55.4
|
1.0
|
O
|
D:ARG108
|
2.5
|
56.6
|
1.0
|
CD
|
D:GLU109
|
3.2
|
56.7
|
1.0
|
CG
|
B:ASP357
|
3.3
|
49.7
|
1.0
|
CG
|
B:ASP353
|
3.3
|
51.7
|
1.0
|
O
|
B:HOH865
|
3.5
|
56.2
|
1.0
|
OD1
|
B:ASP357
|
3.5
|
54.0
|
1.0
|
C
|
D:ARG108
|
3.6
|
49.4
|
1.0
|
OD1
|
B:ASP353
|
3.8
|
58.6
|
1.0
|
CG
|
D:GLU109
|
3.8
|
51.8
|
1.0
|
CB
|
D:ARG108
|
4.1
|
41.8
|
1.0
|
O
|
D:HOH890
|
4.2
|
51.8
|
1.0
|
OE1
|
D:GLU109
|
4.3
|
53.1
|
1.0
|
N
|
D:GLU109
|
4.4
|
44.8
|
1.0
|
CA
|
D:ARG108
|
4.5
|
39.7
|
1.0
|
O
|
D:HOH828
|
4.5
|
48.1
|
1.0
|
O
|
D:PHE107
|
4.5
|
48.4
|
1.0
|
O
|
B:ASP353
|
4.5
|
40.9
|
1.0
|
CA
|
D:GLU109
|
4.5
|
45.2
|
1.0
|
CB
|
B:ASP353
|
4.5
|
41.6
|
1.0
|
CB
|
B:ASP357
|
4.6
|
44.2
|
1.0
|
O
|
D:HOH868
|
4.7
|
57.2
|
1.0
|
NZ
|
C:LYS433
|
4.7
|
53.4
|
1.0
|
CD1
|
C:PHE429
|
4.7
|
50.3
|
1.0
|
CB
|
D:GLU109
|
4.8
|
48.1
|
1.0
|
O
|
D:HOH932
|
4.8
|
49.0
|
1.0
|
C
|
B:ASP353
|
4.8
|
37.4
|
1.0
|
CE
|
C:LYS433
|
5.0
|
53.5
|
1.0
|
|
Iron binding site 9 out
of 32 in 9cqx
Go back to
Iron Binding Sites List in 9cqx
Iron binding site 9 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe602
b:47.3
occ:1.00
|
FE1
|
B:CLF602
|
0.0
|
47.3
|
1.0
|
S3A
|
B:CLF602
|
2.3
|
31.3
|
1.0
|
S2A
|
B:CLF602
|
2.3
|
34.0
|
1.0
|
SG
|
B:CYS95
|
2.3
|
32.4
|
1.0
|
S1
|
B:CLF602
|
2.5
|
47.5
|
1.0
|
FE2
|
B:CLF602
|
2.5
|
48.5
|
1.0
|
FE4
|
B:CLF602
|
2.6
|
55.6
|
1.0
|
FE3
|
B:CLF602
|
2.7
|
48.6
|
1.0
|
FE8
|
B:CLF602
|
3.0
|
48.7
|
1.0
|
N
|
B:CYS95
|
3.2
|
29.6
|
1.0
|
CB
|
B:CYS95
|
3.5
|
23.3
|
1.0
|
CA
|
B:CYS95
|
3.5
|
23.8
|
1.0
|
S4A
|
B:CLF602
|
3.7
|
34.0
|
1.0
|
C
|
B:GLY94
|
3.8
|
27.9
|
1.0
|
S4B
|
B:CLF602
|
4.1
|
31.7
|
1.0
|
CA
|
B:GLY94
|
4.3
|
27.7
|
1.0
|
O
|
B:HOH890
|
4.5
|
41.1
|
1.0
|
O
|
B:GLY94
|
4.6
|
34.3
|
1.0
|
SG
|
A:CYS154
|
4.6
|
39.8
|
1.0
|
CB
|
B:SER92
|
4.6
|
40.6
|
1.0
|
SG
|
A:CYS62
|
4.7
|
32.2
|
1.0
|
N
|
B:GLY94
|
4.7
|
27.9
|
1.0
|
SG
|
A:CYS88
|
5.0
|
46.4
|
1.0
|
FE5
|
B:CLF602
|
5.0
|
60.7
|
1.0
|
|
Iron binding site 10 out
of 32 in 9cqx
Go back to
Iron Binding Sites List in 9cqx
Iron binding site 10 out
of 32 in the Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon
 Mono view
 Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Azotobacter Vinelandii Oxidized Mofep (C1 Symmetry) Obtained Using the Spt Labtech Chameleon within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe602
b:48.5
occ:1.00
|
FE2
|
B:CLF602
|
0.0
|
48.5
|
1.0
|
S2A
|
B:CLF602
|
2.3
|
34.0
|
1.0
|
S4A
|
B:CLF602
|
2.3
|
34.0
|
1.0
|
SG
|
A:CYS154
|
2.3
|
39.8
|
1.0
|
S1
|
B:CLF602
|
2.4
|
47.5
|
1.0
|
FE1
|
B:CLF602
|
2.5
|
47.3
|
1.0
|
FE4
|
B:CLF602
|
2.6
|
55.6
|
1.0
|
FE3
|
B:CLF602
|
2.8
|
48.6
|
1.0
|
CB
|
A:CYS154
|
3.7
|
36.6
|
1.0
|
CA
|
A:GLY185
|
3.7
|
36.7
|
1.0
|
S3A
|
B:CLF602
|
3.8
|
31.3
|
1.0
|
O
|
B:HOH890
|
3.9
|
41.1
|
1.0
|
SG
|
B:CYS95
|
4.0
|
32.4
|
1.0
|
N
|
A:GLY185
|
4.1
|
36.9
|
1.0
|
N
|
A:CYS154
|
4.2
|
36.6
|
1.0
|
FE8
|
B:CLF602
|
4.4
|
48.7
|
1.0
|
CA
|
A:CYS154
|
4.5
|
39.1
|
1.0
|
CB
|
B:SER92
|
4.6
|
40.6
|
1.0
|
OG
|
B:SER92
|
4.7
|
47.0
|
1.0
|
C
|
A:GLY185
|
4.7
|
38.7
|
1.0
|
SG
|
A:CYS62
|
5.0
|
32.2
|
1.0
|
|
Reference:
B.D.Cook,
S.M.Narehood,
K.L.Mcguire,
Y.Li,
F.Akif Tezcan,
M.A.Herzik Jr..
Preparation of Oxygen-Sensitive Proteins For High-Resolution Cryoem Structure Determination Using Blot-Free Vitrification. Nat Commun V. 16 3528 2025.
ISSN: ESSN 2041-1723
PubMed: 40229244
DOI: 10.1038/S41467-025-58243-1
Page generated: Fri Aug 8 03:15:54 2025
|