Iron in PDB 11nd: Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
Enzymatic activity of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
All present enzymatic activity of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact:
1.18.6.1;
Other elements in 11nd:
The structure of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact 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 Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
(pdb code 11nd). 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 Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact, PDB code: 11nd:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 1 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:39.9
occ:1.00
|
FE1
|
A:ICS502
|
0.0
|
39.9
|
1.0
|
|
SG
|
A:CYS275
|
2.2
|
29.2
|
1.0
|
|
S2A
|
A:ICS502
|
2.3
|
24.0
|
1.0
|
|
S4A
|
A:ICS502
|
2.3
|
27.8
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
20.2
|
1.0
|
|
FE4
|
A:ICS502
|
2.7
|
43.5
|
1.0
|
|
FE3
|
A:ICS502
|
2.7
|
37.0
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
33.7
|
1.0
|
|
CB
|
A:CYS275
|
3.3
|
26.0
|
1.0
|
|
CX
|
A:ICS502
|
3.5
|
28.9
|
1.0
|
|
CB
|
A:LEU358
|
4.0
|
36.3
|
1.0
|
|
OG
|
A:SER278
|
4.2
|
29.8
|
1.0
|
|
CB
|
A:SER278
|
4.3
|
22.3
|
1.0
|
|
CE2
|
A:TYR229
|
4.5
|
19.4
|
1.0
|
|
CA
|
A:CYS275
|
4.6
|
26.2
|
1.0
|
|
CD2
|
A:LEU358
|
4.6
|
34.6
|
1.0
|
|
N
|
A:LEU358
|
4.7
|
38.9
|
1.0
|
|
S3A
|
A:ICS502
|
4.8
|
30.6
|
1.0
|
|
S5A
|
A:ICS502
|
4.8
|
34.2
|
1.0
|
|
CG
|
A:LEU358
|
4.9
|
38.3
|
1.0
|
|
S2B
|
A:ICS502
|
4.9
|
24.1
|
1.0
|
|
N
|
A:SER278
|
4.9
|
23.3
|
1.0
|
|
CD2
|
A:TYR229
|
4.9
|
17.1
|
1.0
|
|
FE7
|
A:ICS502
|
5.0
|
35.6
|
1.0
|
|
Iron binding site 2 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 2 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:33.7
occ:1.00
|
FE2
|
A:ICS502
|
0.0
|
33.7
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S2B
|
A:ICS502
|
2.2
|
24.1
|
1.0
|
|
S2A
|
A:ICS502
|
2.2
|
24.0
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
20.2
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
37.4
|
1.0
|
|
FE4
|
A:ICS502
|
2.7
|
43.5
|
1.0
|
|
FE3
|
A:ICS502
|
2.7
|
37.0
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
39.9
|
1.0
|
|
FE5
|
A:ICS502
|
3.7
|
37.6
|
1.0
|
|
FE7
|
A:ICS502
|
3.7
|
35.6
|
1.0
|
|
S4A
|
A:ICS502
|
3.9
|
27.8
|
1.0
|
|
CE1
|
A:HIS195
|
3.9
|
19.2
|
1.0
|
|
CZ
|
A:PHE381
|
4.0
|
24.8
|
1.0
|
|
NE2
|
A:HIS195
|
4.2
|
16.9
|
1.0
|
|
S1B
|
A:ICS502
|
4.2
|
27.3
|
1.0
|
|
S3B
|
A:ICS502
|
4.2
|
28.4
|
1.0
|
|
CG1
|
A:VAL70
|
4.5
|
15.6
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
30.6
|
1.0
|
|
S5A
|
A:ICS502
|
4.6
|
34.2
|
1.0
|
|
SG
|
A:CYS275
|
4.6
|
29.2
|
1.0
|
|
CE2
|
A:PHE381
|
4.6
|
30.4
|
1.0
|
|
CG2
|
A:VAL70
|
4.8
|
14.4
|
1.0
|
|
CE1
|
A:PHE381
|
5.0
|
29.6
|
1.0
|
|
CA
|
A:GLY357
|
5.0
|
33.3
|
1.0
|
|
Iron binding site 3 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 3 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:37.0
occ:1.00
|
FE3
|
A:ICS502
|
0.0
|
37.0
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S5A
|
A:ICS502
|
2.2
|
34.2
|
1.0
|
|
S4A
|
A:ICS502
|
2.2
|
27.8
|
1.0
|
|
S2A
|
A:ICS502
|
2.3
|
24.0
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
35.6
|
1.0
|
|
FE4
|
A:ICS502
|
2.6
|
43.5
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
39.9
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
33.7
|
1.0
|
|
FE6
|
A:ICS502
|
3.7
|
37.4
|
1.0
|
|
FE5
|
A:ICS502
|
3.7
|
37.6
|
1.0
|
|
O
|
A:HOH1015
|
3.8
|
24.3
|
1.0
|
|
S1A
|
A:ICS502
|
3.9
|
20.2
|
1.0
|
|
NH2
|
A:ARG96
|
3.9
|
18.8
|
1.0
|
|
CD2
|
A:TYR229
|
4.1
|
17.1
|
1.0
|
|
S4B
|
A:ICS502
|
4.2
|
23.6
|
1.0
|
|
S3B
|
A:ICS502
|
4.2
|
28.4
|
1.0
|
|
CE2
|
A:TYR229
|
4.4
|
19.4
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
30.6
|
1.0
|
|
S2B
|
A:ICS502
|
4.5
|
24.1
|
1.0
|
|
SG
|
A:CYS275
|
4.7
|
29.2
|
1.0
|
|
NH2
|
A:ARG359
|
4.8
|
23.9
|
1.0
|
|
NE
|
A:ARG359
|
4.9
|
32.1
|
1.0
|
|
CZ
|
A:ARG359
|
5.0
|
25.7
|
1.0
|
|
Iron binding site 4 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 4 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:43.5
occ:1.00
|
FE4
|
A:ICS502
|
0.0
|
43.5
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S3A
|
A:ICS502
|
2.2
|
30.6
|
1.0
|
|
S4A
|
A:ICS502
|
2.3
|
27.8
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
20.2
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
37.6
|
1.0
|
|
FE3
|
A:ICS502
|
2.6
|
37.0
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
39.9
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
33.7
|
1.0
|
|
N
|
A:LEU358
|
3.4
|
38.9
|
1.0
|
|
FE7
|
A:ICS502
|
3.7
|
35.6
|
1.0
|
|
FE6
|
A:ICS502
|
3.7
|
37.4
|
1.0
|
|
S2A
|
A:ICS502
|
3.8
|
24.0
|
1.0
|
|
CB
|
A:LEU358
|
4.0
|
36.3
|
1.0
|
|
CA
|
A:GLY357
|
4.1
|
33.3
|
1.0
|
|
C
|
A:GLY357
|
4.2
|
36.0
|
1.0
|
|
S4B
|
A:ICS502
|
4.2
|
23.6
|
1.0
|
|
S1B
|
A:ICS502
|
4.3
|
27.3
|
1.0
|
|
CA
|
A:LEU358
|
4.3
|
37.9
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
34.2
|
1.0
|
|
S2B
|
A:ICS502
|
4.5
|
24.1
|
1.0
|
|
SG
|
A:CYS275
|
4.5
|
29.2
|
1.0
|
|
N
|
A:ARG359
|
4.5
|
37.1
|
1.0
|
|
O
|
A:GLY356
|
4.6
|
51.0
|
1.0
|
|
CG
|
A:ARG359
|
4.9
|
34.0
|
1.0
|
|
CD2
|
A:LEU358
|
4.9
|
34.6
|
1.0
|
|
NE
|
A:ARG359
|
4.9
|
32.1
|
1.0
|
|
CD
|
A:ARG359
|
4.9
|
30.9
|
1.0
|
|
C
|
A:LEU358
|
5.0
|
40.5
|
1.0
|
|
Iron binding site 5 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 5 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:37.6
occ:1.00
|
FE5
|
A:ICS502
|
0.0
|
37.6
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S4B
|
A:ICS502
|
2.2
|
23.6
|
1.0
|
|
S3A
|
A:ICS502
|
2.2
|
30.6
|
1.0
|
|
S1B
|
A:ICS502
|
2.3
|
27.3
|
1.0
|
|
FE4
|
A:ICS502
|
2.6
|
43.5
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
37.4
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
35.6
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
44.4
|
1.0
|
|
FE3
|
A:ICS502
|
3.7
|
37.0
|
1.0
|
|
FE2
|
A:ICS502
|
3.7
|
33.7
|
1.0
|
|
S3B
|
A:ICS502
|
3.9
|
28.4
|
1.0
|
|
CD2
|
A:HIS442
|
4.3
|
25.7
|
1.0
|
|
S4A
|
A:ICS502
|
4.3
|
27.8
|
1.0
|
|
S1A
|
A:ICS502
|
4.3
|
20.2
|
1.0
|
|
S2B
|
A:ICS502
|
4.4
|
24.1
|
1.0
|
|
S5A
|
A:ICS502
|
4.4
|
34.2
|
1.0
|
|
O
|
A:GLY356
|
4.5
|
51.0
|
1.0
|
|
O
|
A:ILE355
|
4.5
|
42.9
|
1.0
|
|
CD
|
A:ARG359
|
4.7
|
30.9
|
1.0
|
|
CG2
|
A:ILE355
|
4.9
|
37.9
|
1.0
|
|
NE2
|
A:HIS442
|
4.9
|
30.4
|
1.0
|
|
CA
|
A:GLY357
|
4.9
|
33.3
|
1.0
|
|
CG
|
A:HIS442
|
4.9
|
26.3
|
1.0
|
|
NE
|
A:ARG359
|
5.0
|
32.1
|
1.0
|
|
Iron binding site 6 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 6 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:37.4
occ:1.00
|
FE6
|
A:ICS502
|
0.0
|
37.4
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S2B
|
A:ICS502
|
2.2
|
24.1
|
1.0
|
|
S3B
|
A:ICS502
|
2.2
|
28.4
|
1.0
|
|
S1B
|
A:ICS502
|
2.2
|
27.3
|
1.0
|
|
FE2
|
A:ICS502
|
2.6
|
33.7
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
35.6
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
37.6
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
44.4
|
1.0
|
|
FE3
|
A:ICS502
|
3.7
|
37.0
|
1.0
|
|
FE4
|
A:ICS502
|
3.7
|
43.5
|
1.0
|
|
S4B
|
A:ICS502
|
3.8
|
23.6
|
1.0
|
|
O7
|
A:HCA501
|
4.0
|
31.9
|
1.0
|
|
S2A
|
A:ICS502
|
4.2
|
24.0
|
1.0
|
|
O1
|
A:HCA501
|
4.3
|
35.8
|
1.0
|
|
S1A
|
A:ICS502
|
4.3
|
20.2
|
1.0
|
|
CZ
|
A:PHE381
|
4.4
|
24.8
|
1.0
|
|
CG2
|
A:VAL70
|
4.4
|
14.4
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
34.2
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
30.6
|
1.0
|
|
CE1
|
A:PHE381
|
4.7
|
29.6
|
1.0
|
|
O5
|
A:HCA501
|
4.9
|
27.2
|
1.0
|
|
NE
|
A:ARG96
|
5.0
|
22.6
|
1.0
|
|
Iron binding site 7 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 7 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:35.6
occ:1.00
|
FE7
|
A:ICS502
|
0.0
|
35.6
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
28.9
|
1.0
|
|
S4B
|
A:ICS502
|
2.2
|
23.6
|
1.0
|
|
S5A
|
A:ICS502
|
2.2
|
34.2
|
1.0
|
|
S3B
|
A:ICS502
|
2.3
|
28.4
|
1.0
|
|
FE3
|
A:ICS502
|
2.6
|
37.0
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
37.4
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
37.6
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
44.4
|
1.0
|
|
O
|
A:HOH772
|
3.3
|
21.9
|
1.0
|
|
FE2
|
A:ICS502
|
3.7
|
33.7
|
1.0
|
|
FE4
|
A:ICS502
|
3.7
|
43.5
|
1.0
|
|
S1B
|
A:ICS502
|
3.8
|
27.3
|
1.0
|
|
NE
|
A:ARG96
|
4.0
|
22.6
|
1.0
|
|
NH2
|
A:ARG96
|
4.0
|
18.8
|
1.0
|
|
O5
|
A:HCA501
|
4.2
|
27.2
|
1.0
|
|
S2A
|
A:ICS502
|
4.2
|
24.0
|
1.0
|
|
S4A
|
A:ICS502
|
4.3
|
27.8
|
1.0
|
|
S2B
|
A:ICS502
|
4.4
|
24.1
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
30.6
|
1.0
|
|
CZ
|
A:ARG96
|
4.5
|
20.9
|
1.0
|
|
CZ
|
A:ARG359
|
4.6
|
25.7
|
1.0
|
|
NH1
|
A:ARG359
|
4.7
|
25.6
|
1.0
|
|
NH2
|
A:ARG359
|
4.8
|
23.9
|
1.0
|
|
O7
|
A:HCA501
|
4.9
|
31.9
|
1.0
|
|
FE1
|
A:ICS502
|
5.0
|
39.9
|
1.0
|
|
Iron binding site 8 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 8 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:48.7
occ:1.00
|
OE2
|
D:GLU109
|
2.1
|
26.6
|
1.0
|
|
O
|
D:ARG108
|
2.2
|
20.2
|
1.0
|
|
OD2
|
B:ASP357
|
2.4
|
22.8
|
1.0
|
|
OD2
|
B:ASP353
|
2.4
|
22.6
|
1.0
|
|
O
|
D:HOH973
|
2.5
|
17.6
|
1.0
|
|
OD1
|
B:ASP353
|
3.1
|
23.1
|
1.0
|
|
CG
|
B:ASP353
|
3.1
|
20.4
|
1.0
|
|
CD
|
D:GLU109
|
3.2
|
26.2
|
1.0
|
|
CG
|
B:ASP357
|
3.3
|
21.9
|
1.0
|
|
C
|
D:ARG108
|
3.4
|
15.8
|
1.0
|
|
OD1
|
B:ASP357
|
3.4
|
24.5
|
1.0
|
|
CG
|
D:GLU109
|
3.6
|
22.6
|
1.0
|
|
CB
|
D:ARG108
|
4.1
|
15.4
|
1.0
|
|
N
|
D:GLU109
|
4.2
|
17.4
|
1.0
|
|
CA
|
D:GLU109
|
4.3
|
17.3
|
1.0
|
|
OE1
|
D:GLU109
|
4.3
|
27.5
|
1.0
|
|
NZ
|
C:LYS433
|
4.3
|
19.2
|
1.0
|
|
CA
|
D:ARG108
|
4.3
|
16.8
|
1.0
|
|
O
|
D:PHE107
|
4.3
|
17.5
|
1.0
|
|
O
|
B:HOH798
|
4.5
|
22.8
|
1.0
|
|
CD1
|
C:PHE429
|
4.5
|
25.0
|
1.0
|
|
CB
|
D:GLU109
|
4.5
|
21.2
|
1.0
|
|
O
|
D:HOH824
|
4.6
|
27.1
|
1.0
|
|
CB
|
B:ASP353
|
4.6
|
14.9
|
1.0
|
|
O
|
D:HOH917
|
4.6
|
26.1
|
1.0
|
|
O
|
B:ASP353
|
4.6
|
17.1
|
1.0
|
|
O
|
B:HOH894
|
4.7
|
29.1
|
1.0
|
|
CB
|
B:ASP357
|
4.7
|
18.9
|
1.0
|
|
CE
|
C:LYS433
|
4.7
|
16.8
|
1.0
|
|
O
|
D:HOH1112
|
4.9
|
25.0
|
1.0
|
|
C
|
B:ASP353
|
5.0
|
16.1
|
1.0
|
|
CE1
|
C:PHE429
|
5.0
|
22.8
|
1.0
|
|
Iron binding site 9 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 9 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe602
b:18.6
occ:1.00
|
FE1
|
B:CLF602
|
0.0
|
18.6
|
1.0
|
|
SG
|
A:CYS154
|
2.2
|
13.7
|
1.0
|
|
S2A
|
B:CLF602
|
2.3
|
5.9
|
1.0
|
|
S3A
|
B:CLF602
|
2.3
|
17.1
|
1.0
|
|
S1
|
B:CLF602
|
2.4
|
14.3
|
1.0
|
|
FE2
|
B:CLF602
|
2.5
|
25.1
|
1.0
|
|
FE4
|
B:CLF602
|
2.6
|
26.9
|
1.0
|
|
FE3
|
B:CLF602
|
2.8
|
16.9
|
1.0
|
|
CB
|
A:CYS154
|
3.4
|
11.1
|
1.0
|
|
O
|
B:HOH1071
|
3.6
|
3.8
|
1.0
|
|
OG
|
B:SER92
|
3.8
|
21.9
|
1.0
|
|
S4A
|
B:CLF602
|
3.8
|
11.9
|
1.0
|
|
CA
|
A:GLY185
|
3.9
|
10.6
|
1.0
|
|
N
|
A:CYS154
|
4.0
|
11.3
|
1.0
|
|
N
|
A:GLY185
|
4.1
|
12.3
|
1.0
|
|
SG
|
B:CYS95
|
4.2
|
15.7
|
1.0
|
|
CA
|
A:CYS154
|
4.3
|
12.8
|
1.0
|
|
FE8
|
B:CLF602
|
4.4
|
25.4
|
1.0
|
|
FE5
|
B:CLF602
|
4.6
|
34.4
|
1.0
|
|
SG
|
A:CYS88
|
4.6
|
11.5
|
1.0
|
|
C
|
A:GLY185
|
4.7
|
16.5
|
1.0
|
|
CB
|
B:SER92
|
4.8
|
17.5
|
1.0
|
|
FE6
|
B:CLF602
|
4.9
|
41.8
|
1.0
|
|
SG
|
A:CYS62
|
4.9
|
8.4
|
1.0
|
|
N
|
A:PHE186
|
5.0
|
14.3
|
1.0
|
|
Iron binding site 10 out
of 32 in 11nd
Go back to
Iron Binding Sites List in 11nd
Iron binding site 10 out
of 32 in the Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Azotobacter Vinelandii Mofep (C2 Symmetry) Determined Using the Spt Labtech Chameleon in the Presence of 0.25X Surfact within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe602
b:25.1
occ:1.00
|
FE2
|
B:CLF602
|
0.0
|
25.1
|
1.0
|
|
S4A
|
B:CLF602
|
2.3
|
11.9
|
1.0
|
|
S2A
|
B:CLF602
|
2.3
|
5.9
|
1.0
|
|
SG
|
B:CYS95
|
2.3
|
15.7
|
1.0
|
|
S1
|
B:CLF602
|
2.5
|
14.3
|
1.0
|
|
FE1
|
B:CLF602
|
2.5
|
18.6
|
1.0
|
|
FE4
|
B:CLF602
|
2.6
|
26.9
|
1.0
|
|
FE3
|
B:CLF602
|
2.8
|
16.9
|
1.0
|
|
FE8
|
B:CLF602
|
2.9
|
25.4
|
1.0
|
|
N
|
B:CYS95
|
3.3
|
11.6
|
1.0
|
|
CB
|
B:CYS95
|
3.5
|
10.2
|
1.0
|
|
CA
|
B:CYS95
|
3.6
|
9.5
|
1.0
|
|
OG
|
B:SER92
|
3.7
|
21.9
|
1.0
|
|
S3A
|
B:CLF602
|
3.8
|
17.1
|
1.0
|
|
FE5
|
B:CLF602
|
3.8
|
34.4
|
1.0
|
|
S4B
|
B:CLF602
|
3.9
|
7.6
|
1.0
|
|
C
|
B:GLY94
|
4.0
|
10.7
|
1.0
|
|
O
|
B:HOH1071
|
4.1
|
3.8
|
1.0
|
|
SG
|
A:CYS154
|
4.5
|
13.7
|
1.0
|
|
CA
|
B:GLY94
|
4.5
|
9.5
|
1.0
|
|
SG
|
A:CYS88
|
4.5
|
11.5
|
1.0
|
|
FE6
|
B:CLF602
|
4.6
|
41.8
|
1.0
|
|
O
|
B:GLY94
|
4.7
|
12.8
|
1.0
|
|
SG
|
A:CYS62
|
4.8
|
8.4
|
1.0
|
|
N
|
B:GLY94
|
4.9
|
13.3
|
1.0
|
|
CB
|
B:SER92
|
5.0
|
17.5
|
1.0
|
|
Reference:
S.E.Enos,
B.D.Cook,
H.Rahmani,
S.M.Narehood,
Y.Li,
I.C.Kuschnerus,
T.H.Redford,
P.Dukakis,
D.Ji,
M.J.Bachochin,
D.A.Grotjahn,
M.A.Herzik.
A Surfactant Cocktail Overcomes Air-Water Interface Artifacts in Single-Particle Cryoem. Biorxiv 2026.
ISSN: ISSN 2692-8205
PubMed: 41889805
DOI: 10.64898/2026.03.17.712260
Page generated: Sun Oct 4 08:33:22 2026
|