Iron in PDB 7uta: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction:
1.18.6.1;
Other elements in 7uta:
The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction 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 -
40;
Binding sites:
The binding sites of Iron atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
(pdb code 7uta). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 40 binding sites of Iron where determined in the
Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction, PDB code: 7uta:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 1 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE1
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
S2A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
SG
|
A:CYS275
|
2.3
|
26.6
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
CB
|
A:CYS275
|
3.3
|
32.7
|
1.0
|
CX
|
A:ICS502
|
3.5
|
53.3
|
1.0
|
CB
|
A:LEU358
|
4.2
|
53.5
|
1.0
|
OG
|
A:SER278
|
4.2
|
32.9
|
1.0
|
CB
|
A:SER278
|
4.4
|
31.6
|
1.0
|
CE2
|
A:TYR229
|
4.5
|
25.0
|
1.0
|
CA
|
A:CYS275
|
4.5
|
28.1
|
1.0
|
CD2
|
A:LEU358
|
4.8
|
53.0
|
1.0
|
S2B
|
A:ICS502
|
4.8
|
53.3
|
1.0
|
S3A
|
A:ICS502
|
4.8
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
4.8
|
53.3
|
1.0
|
N
|
A:LEU358
|
4.9
|
55.9
|
1.0
|
N
|
A:SER278
|
5.0
|
25.7
|
1.0
|
FE7
|
A:ICS502
|
5.0
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
5.0
|
53.3
|
1.0
|
|
Iron binding site 2 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 2 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE2
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S2B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S2A
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE5
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE7
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S4A
|
A:ICS502
|
3.9
|
53.3
|
1.0
|
CE1
|
A:HIS195
|
4.1
|
25.8
|
1.0
|
CZ
|
A:PHE381
|
4.2
|
64.9
|
1.0
|
S3B
|
A:ICS502
|
4.2
|
53.3
|
1.0
|
S1B
|
A:ICS502
|
4.2
|
53.3
|
1.0
|
NE2
|
A:HIS195
|
4.3
|
26.4
|
1.0
|
CE1
|
A:PHE381
|
4.4
|
66.2
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
CG1
|
A:VAL70
|
4.5
|
25.0
|
1.0
|
SG
|
A:CYS275
|
4.6
|
26.6
|
1.0
|
CG2
|
A:VAL70
|
4.9
|
26.1
|
1.0
|
N
|
A:GLY357
|
4.9
|
63.9
|
1.0
|
|
Iron binding site 3 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 3 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE3
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S4A
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S2A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE5
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S1A
|
A:ICS502
|
3.9
|
53.3
|
1.0
|
CD2
|
A:TYR229
|
4.1
|
24.4
|
1.0
|
CE2
|
A:TYR229
|
4.2
|
25.0
|
1.0
|
S3B
|
A:ICS502
|
4.2
|
53.3
|
1.0
|
S4B
|
A:ICS502
|
4.2
|
53.3
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
NH1
|
A:ARG96
|
4.6
|
33.4
|
1.0
|
SG
|
A:CYS275
|
4.7
|
26.6
|
1.0
|
NE
|
A:ARG359
|
4.9
|
58.6
|
1.0
|
NH2
|
A:ARG359
|
5.0
|
56.1
|
1.0
|
|
Iron binding site 4 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 4 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE4
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S3A
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
S1A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE7
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S2A
|
A:ICS502
|
3.8
|
53.3
|
1.0
|
N
|
A:LEU358
|
3.9
|
55.9
|
1.0
|
N
|
A:GLY357
|
3.9
|
63.9
|
1.0
|
CB
|
A:LEU358
|
4.2
|
53.5
|
1.0
|
S4B
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
S1B
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
N
|
A:ARG359
|
4.6
|
58.6
|
1.0
|
CA
|
A:LEU358
|
4.6
|
55.6
|
1.0
|
C
|
A:GLY356
|
4.7
|
70.7
|
1.0
|
CA
|
A:GLY357
|
4.7
|
62.7
|
1.0
|
SG
|
A:CYS275
|
4.7
|
26.6
|
1.0
|
C
|
A:GLY357
|
4.8
|
62.4
|
1.0
|
CA
|
A:GLY356
|
4.8
|
68.8
|
1.0
|
CG
|
A:ARG359
|
4.8
|
57.6
|
1.0
|
CD
|
A:ARG359
|
4.8
|
58.8
|
1.0
|
NE
|
A:ARG359
|
4.8
|
58.6
|
1.0
|
|
Iron binding site 5 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 5 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE5
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S4B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S3A
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
S1B
|
A:ICS502
|
2.3
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S3B
|
A:ICS502
|
3.9
|
53.3
|
1.0
|
N
|
A:GLY356
|
4.0
|
69.5
|
1.0
|
CA
|
A:GLY356
|
4.1
|
68.8
|
1.0
|
S1A
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
CG2
|
A:ILE355
|
4.3
|
70.7
|
1.0
|
S4A
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
CD
|
A:ARG359
|
4.4
|
58.8
|
1.0
|
S2B
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
ND1
|
A:HIS442
|
4.5
|
54.2
|
1.0
|
NE
|
A:ARG359
|
4.6
|
58.6
|
1.0
|
N
|
A:GLY357
|
4.7
|
63.9
|
1.0
|
CE1
|
A:HIS442
|
4.8
|
56.2
|
1.0
|
C
|
A:GLY356
|
4.9
|
70.7
|
1.0
|
CZ
|
A:ARG359
|
4.9
|
57.8
|
1.0
|
CZ
|
A:PHE381
|
4.9
|
64.9
|
1.0
|
|
Iron binding site 6 out
of 40 in 7uta
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Iron Binding Sites List in 7uta
Iron binding site 6 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE6
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S2B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S3B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S1B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE7
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S4B
|
A:ICS502
|
3.8
|
53.3
|
1.0
|
O2
|
A:HCA501
|
3.9
|
61.2
|
1.0
|
CZ
|
A:PHE381
|
4.2
|
64.9
|
1.0
|
S2A
|
A:ICS502
|
4.2
|
53.3
|
1.0
|
O7
|
A:HCA501
|
4.3
|
55.9
|
1.0
|
S1A
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
CG2
|
A:VAL70
|
4.5
|
26.1
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
NH1
|
A:ARG96
|
4.7
|
33.4
|
1.0
|
CE2
|
A:PHE381
|
4.8
|
66.5
|
1.0
|
O5
|
A:HCA501
|
4.9
|
57.1
|
1.0
|
C1
|
A:HCA501
|
4.9
|
59.8
|
1.0
|
FE1
|
A:ICS502
|
5.0
|
53.3
|
1.0
|
|
Iron binding site 7 out
of 40 in 7uta
Go back to
Iron Binding Sites List in 7uta
Iron binding site 7 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:53.3
occ:1.00
|
FE7
|
A:ICS502
|
0.0
|
53.3
|
1.0
|
CX
|
A:ICS502
|
2.0
|
53.3
|
1.0
|
S5A
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S4B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
S3B
|
A:ICS502
|
2.2
|
53.3
|
1.0
|
FE3
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE6
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
FE5
|
A:ICS502
|
2.6
|
53.3
|
1.0
|
MO1
|
A:ICS502
|
2.7
|
53.3
|
1.0
|
FE2
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
FE4
|
A:ICS502
|
3.7
|
53.3
|
1.0
|
S1B
|
A:ICS502
|
3.8
|
53.3
|
1.0
|
NH1
|
A:ARG96
|
4.1
|
33.4
|
1.0
|
S2A
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
S4A
|
A:ICS502
|
4.3
|
53.3
|
1.0
|
CZ
|
A:ARG359
|
4.4
|
57.8
|
1.0
|
S2B
|
A:ICS502
|
4.4
|
53.3
|
1.0
|
NH2
|
A:ARG359
|
4.4
|
56.1
|
1.0
|
O5
|
A:HCA501
|
4.5
|
57.1
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
53.3
|
1.0
|
NE
|
A:ARG359
|
4.6
|
58.6
|
1.0
|
NH1
|
A:ARG359
|
4.7
|
58.4
|
1.0
|
CD
|
A:ARG96
|
4.8
|
29.6
|
1.0
|
CZ
|
A:ARG96
|
4.9
|
31.3
|
1.0
|
FE1
|
A:ICS502
|
5.0
|
53.3
|
1.0
|
|
Iron binding site 8 out
of 40 in 7uta
Go back to
Iron Binding Sites List in 7uta
Iron binding site 8 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:27.0
occ:1.00
|
FE1
|
B:CLF601
|
0.0
|
27.0
|
1.0
|
S3A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
S2A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
SG
|
B:CYS95
|
2.3
|
20.1
|
1.0
|
S1
|
B:CLF601
|
2.5
|
27.0
|
1.0
|
FE2
|
B:CLF601
|
2.5
|
27.0
|
1.0
|
FE4
|
B:CLF601
|
2.6
|
27.0
|
1.0
|
FE3
|
B:CLF601
|
2.7
|
27.0
|
1.0
|
FE8
|
B:CLF601
|
3.0
|
27.0
|
1.0
|
N
|
B:CYS95
|
3.1
|
21.6
|
1.0
|
CB
|
B:CYS95
|
3.5
|
22.4
|
1.0
|
CA
|
B:CYS95
|
3.5
|
19.3
|
1.0
|
S4A
|
B:CLF601
|
3.7
|
27.0
|
1.0
|
C
|
B:GLY94
|
3.8
|
21.0
|
1.0
|
FE5
|
B:CLF601
|
3.8
|
27.0
|
1.0
|
S4B
|
B:CLF601
|
3.9
|
27.0
|
1.0
|
CA
|
B:GLY94
|
4.3
|
19.3
|
1.0
|
O
|
B:HOH726
|
4.3
|
26.9
|
1.0
|
O
|
B:GLY94
|
4.5
|
32.1
|
1.0
|
CB
|
B:SER92
|
4.5
|
32.5
|
1.0
|
SG
|
A:CYS154
|
4.6
|
9.8
|
1.0
|
N
|
B:GLY94
|
4.7
|
21.6
|
1.0
|
SG
|
A:CYS62
|
4.7
|
20.2
|
1.0
|
SG
|
A:CYS88
|
4.8
|
21.1
|
1.0
|
FE6
|
B:CLF601
|
4.8
|
27.0
|
1.0
|
|
Iron binding site 9 out
of 40 in 7uta
Go back to
Iron Binding Sites List in 7uta
Iron binding site 9 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:27.0
occ:1.00
|
FE2
|
B:CLF601
|
0.0
|
27.0
|
1.0
|
S2A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
SG
|
A:CYS154
|
2.3
|
9.8
|
1.0
|
S4A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
S1
|
B:CLF601
|
2.4
|
27.0
|
1.0
|
FE1
|
B:CLF601
|
2.5
|
27.0
|
1.0
|
FE4
|
B:CLF601
|
2.6
|
27.0
|
1.0
|
FE3
|
B:CLF601
|
2.8
|
27.0
|
1.0
|
O
|
B:HOH726
|
3.5
|
26.9
|
1.0
|
CB
|
A:CYS154
|
3.7
|
13.6
|
1.0
|
CA
|
A:GLY185
|
3.8
|
21.7
|
1.0
|
S3A
|
B:CLF601
|
3.8
|
27.0
|
1.0
|
N
|
A:GLY185
|
3.9
|
20.4
|
1.0
|
SG
|
B:CYS95
|
4.1
|
20.1
|
1.0
|
N
|
A:CYS154
|
4.2
|
10.2
|
1.0
|
FE8
|
B:CLF601
|
4.4
|
27.0
|
1.0
|
FE5
|
B:CLF601
|
4.5
|
27.0
|
1.0
|
CB
|
B:SER92
|
4.5
|
32.5
|
1.0
|
CA
|
A:CYS154
|
4.6
|
17.4
|
1.0
|
OG
|
B:SER92
|
4.6
|
34.8
|
1.0
|
C
|
A:GLY185
|
4.7
|
19.1
|
1.0
|
SG
|
A:CYS62
|
4.8
|
20.2
|
1.0
|
SG
|
A:CYS88
|
4.9
|
21.1
|
1.0
|
FE6
|
B:CLF601
|
5.0
|
27.0
|
1.0
|
|
Iron binding site 10 out
of 40 in 7uta
Go back to
Iron Binding Sites List in 7uta
Iron binding site 10 out
of 40 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:27.0
occ:1.00
|
FE3
|
B:CLF601
|
0.0
|
27.0
|
1.0
|
SG
|
A:CYS62
|
2.2
|
20.2
|
1.0
|
S3A
|
B:CLF601
|
2.2
|
27.0
|
1.0
|
S2A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
S4A
|
B:CLF601
|
2.3
|
27.0
|
1.0
|
FE4
|
B:CLF601
|
2.7
|
27.0
|
1.0
|
FE1
|
B:CLF601
|
2.7
|
27.0
|
1.0
|
FE2
|
B:CLF601
|
2.8
|
27.0
|
1.0
|
CB
|
A:CYS62
|
3.2
|
24.0
|
1.0
|
CA
|
A:GLY185
|
3.9
|
21.7
|
1.0
|
CB
|
A:TYR64
|
4.0
|
15.8
|
1.0
|
S1
|
B:CLF601
|
4.2
|
27.0
|
1.0
|
CA
|
B:GLY94
|
4.3
|
19.3
|
1.0
|
N
|
A:GLY185
|
4.5
|
20.4
|
1.0
|
C
|
B:GLY94
|
4.5
|
21.0
|
1.0
|
CG
|
A:TYR64
|
4.6
|
20.8
|
1.0
|
CD1
|
A:TYR64
|
4.6
|
21.9
|
1.0
|
N
|
B:CYS95
|
4.7
|
21.6
|
1.0
|
CA
|
A:CYS62
|
4.7
|
19.5
|
1.0
|
SG
|
A:CYS88
|
4.7
|
21.1
|
1.0
|
SG
|
A:CYS154
|
4.8
|
9.8
|
1.0
|
N
|
A:TYR64
|
4.8
|
19.7
|
1.0
|
CE2
|
B:TYR98
|
5.0
|
14.5
|
1.0
|
|
Reference:
H.L.Rutledge,
B.D.Cook,
H.P.M.Nguyen,
M.A.Herzik Jr.,
F.A.Tezcan.
Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641
Page generated: Fri Aug 9 03:04:21 2024
|