Iron in PDB 10zn: Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
Enzymatic activity of Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
All present enzymatic activity of Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry):
1.18.6.1;
Other elements in 10zn:
The structure of Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
(pdb code 10zn). 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry), PDB code: 10zn:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 1 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:75.3
occ:1.00
|
FE1
|
A:ICS502
|
0.0
|
75.3
|
1.0
|
|
SG
|
A:CYS291
|
2.3
|
64.4
|
1.0
|
|
S2A
|
A:ICS502
|
2.3
|
72.4
|
1.0
|
|
S4A
|
A:ICS502
|
2.3
|
64.7
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
81.1
|
1.0
|
|
FE4
|
A:ICS502
|
2.7
|
80.9
|
1.0
|
|
FE3
|
A:ICS502
|
2.7
|
74.7
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
92.8
|
1.0
|
|
CX
|
A:ICS502
|
3.4
|
78.7
|
1.0
|
|
OG
|
A:SER294
|
3.5
|
54.4
|
1.0
|
|
CB
|
A:CYS291
|
3.5
|
56.7
|
1.0
|
|
CB
|
A:SER294
|
4.1
|
58.1
|
1.0
|
|
CB
|
A:LEU374
|
4.3
|
63.9
|
1.0
|
|
CE2
|
A:TYR245
|
4.5
|
65.6
|
1.0
|
|
N
|
A:SER294
|
4.7
|
64.0
|
1.0
|
|
CA
|
A:CYS291
|
4.8
|
59.4
|
1.0
|
|
S2B
|
A:ICS502
|
4.8
|
68.2
|
1.0
|
|
S3A
|
A:ICS502
|
4.8
|
62.3
|
1.0
|
|
S5A
|
A:ICS502
|
4.8
|
62.6
|
1.0
|
|
CD2
|
A:LEU374
|
4.8
|
62.0
|
1.0
|
|
CB
|
A:ARG293
|
4.9
|
60.6
|
1.0
|
|
FE6
|
A:ICS502
|
5.0
|
86.5
|
1.0
|
|
FE7
|
A:ICS502
|
5.0
|
70.1
|
1.0
|
|
Iron binding site 2 out
of 40 in 10zn
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Iron Binding Sites List in 10zn
Iron binding site 2 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:92.8
occ:1.00
|
FE2
|
A:ICS502
|
0.0
|
92.8
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S2B
|
A:ICS502
|
2.2
|
68.2
|
1.0
|
|
S2A
|
A:ICS502
|
2.2
|
72.4
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
81.1
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
86.5
|
1.0
|
|
FE4
|
A:ICS502
|
2.7
|
80.9
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
75.3
|
1.0
|
|
FE3
|
A:ICS502
|
2.7
|
74.7
|
1.0
|
|
FE5
|
A:ICS502
|
3.7
|
79.6
|
1.0
|
|
FE7
|
A:ICS502
|
3.7
|
70.1
|
1.0
|
|
S4A
|
A:ICS502
|
3.9
|
64.7
|
1.0
|
|
CE1
|
A:HIS211
|
4.0
|
55.1
|
1.0
|
|
NE2
|
A:HIS211
|
4.1
|
53.3
|
1.0
|
|
S3B
|
A:ICS502
|
4.2
|
76.0
|
1.0
|
|
S1B
|
A:ICS502
|
4.2
|
65.9
|
1.0
|
|
CZ
|
A:PHE397
|
4.2
|
62.9
|
1.0
|
|
CE1
|
A:PHE397
|
4.4
|
64.5
|
1.0
|
|
CG1
|
A:VAL86
|
4.5
|
55.9
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
62.3
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
62.6
|
1.0
|
|
SG
|
A:CYS291
|
4.8
|
64.4
|
1.0
|
|
OG
|
A:SER294
|
4.9
|
54.4
|
1.0
|
|
CB
|
A:SER294
|
4.9
|
58.1
|
1.0
|
|
Iron binding site 3 out
of 40 in 10zn
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Iron Binding Sites List in 10zn
Iron binding site 3 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:74.7
occ:1.00
|
FE3
|
A:ICS502
|
0.0
|
74.7
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S5A
|
A:ICS502
|
2.2
|
62.6
|
1.0
|
|
S4A
|
A:ICS502
|
2.2
|
64.7
|
1.0
|
|
S2A
|
A:ICS502
|
2.3
|
72.4
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
70.1
|
1.0
|
|
FE4
|
A:ICS502
|
2.6
|
80.9
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
75.3
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
92.8
|
1.0
|
|
FE6
|
A:ICS502
|
3.7
|
86.5
|
1.0
|
|
FE5
|
A:ICS502
|
3.7
|
79.6
|
1.0
|
|
S1A
|
A:ICS502
|
3.9
|
81.1
|
1.0
|
|
S3B
|
A:ICS502
|
4.2
|
76.0
|
1.0
|
|
S4B
|
A:ICS502
|
4.2
|
75.1
|
1.0
|
|
CD2
|
A:TYR245
|
4.2
|
63.4
|
1.0
|
|
NH2
|
A:ARG112
|
4.3
|
63.0
|
1.0
|
|
CE2
|
A:TYR245
|
4.3
|
65.6
|
1.0
|
|
S2B
|
A:ICS502
|
4.5
|
68.2
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
62.3
|
1.0
|
|
SG
|
A:CYS291
|
4.7
|
64.4
|
1.0
|
|
NH2
|
A:ARG375
|
5.0
|
60.4
|
1.0
|
|
Iron binding site 4 out
of 40 in 10zn
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Iron Binding Sites List in 10zn
Iron binding site 4 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:80.9
occ:1.00
|
FE4
|
A:ICS502
|
0.0
|
80.9
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S3A
|
A:ICS502
|
2.2
|
62.3
|
1.0
|
|
S4A
|
A:ICS502
|
2.3
|
64.7
|
1.0
|
|
S1A
|
A:ICS502
|
2.3
|
81.1
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
79.6
|
1.0
|
|
FE3
|
A:ICS502
|
2.6
|
74.7
|
1.0
|
|
FE1
|
A:ICS502
|
2.7
|
75.3
|
1.0
|
|
FE2
|
A:ICS502
|
2.7
|
92.8
|
1.0
|
|
FE7
|
A:ICS502
|
3.7
|
70.1
|
1.0
|
|
FE6
|
A:ICS502
|
3.7
|
86.5
|
1.0
|
|
S2A
|
A:ICS502
|
3.8
|
72.4
|
1.0
|
|
N
|
A:LEU374
|
3.8
|
62.9
|
1.0
|
|
CB
|
A:LEU374
|
3.9
|
63.9
|
1.0
|
|
N
|
A:GLY373
|
4.0
|
64.7
|
1.0
|
|
S4B
|
A:ICS502
|
4.3
|
75.1
|
1.0
|
|
S1B
|
A:ICS502
|
4.3
|
65.9
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
62.6
|
1.0
|
|
CA
|
A:LEU374
|
4.5
|
62.6
|
1.0
|
|
S2B
|
A:ICS502
|
4.5
|
68.2
|
1.0
|
|
SG
|
A:CYS291
|
4.5
|
64.4
|
1.0
|
|
C
|
A:GLY373
|
4.5
|
60.1
|
1.0
|
|
CA
|
A:GLY373
|
4.6
|
61.3
|
1.0
|
|
N
|
A:ARG375
|
4.8
|
59.2
|
1.0
|
|
CG
|
A:ARG375
|
4.9
|
63.7
|
1.0
|
|
Iron binding site 5 out
of 40 in 10zn
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Iron Binding Sites List in 10zn
Iron binding site 5 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:79.6
occ:1.00
|
FE5
|
A:ICS502
|
0.0
|
79.6
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S4B
|
A:ICS502
|
2.2
|
75.1
|
1.0
|
|
S3A
|
A:ICS502
|
2.3
|
62.3
|
1.0
|
|
S1B
|
A:ICS502
|
2.3
|
65.9
|
1.0
|
|
FE4
|
A:ICS502
|
2.6
|
80.9
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
70.1
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
86.5
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
80.2
|
1.0
|
|
FE2
|
A:ICS502
|
3.7
|
92.8
|
1.0
|
|
FE3
|
A:ICS502
|
3.7
|
74.7
|
1.0
|
|
S3B
|
A:ICS502
|
3.9
|
76.0
|
1.0
|
|
CG1
|
A:VAL371
|
4.0
|
63.1
|
1.0
|
|
N
|
A:GLY372
|
4.2
|
63.9
|
1.0
|
|
S1A
|
A:ICS502
|
4.3
|
81.1
|
1.0
|
|
ND1
|
A:HIS458
|
4.3
|
62.7
|
1.0
|
|
S4A
|
A:ICS502
|
4.3
|
64.7
|
1.0
|
|
CA
|
A:GLY372
|
4.3
|
61.4
|
1.0
|
|
S2B
|
A:ICS502
|
4.5
|
68.2
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
62.6
|
1.0
|
|
CE1
|
A:HIS458
|
4.5
|
62.1
|
1.0
|
|
N
|
A:GLY373
|
4.6
|
64.7
|
1.0
|
|
CD
|
A:ARG375
|
4.7
|
65.9
|
1.0
|
|
NE
|
A:ARG375
|
4.8
|
68.7
|
1.0
|
|
C
|
A:GLY372
|
5.0
|
66.5
|
1.0
|
|
Iron binding site 6 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 6 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:86.5
occ:1.00
|
FE6
|
A:ICS502
|
0.0
|
86.5
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S2B
|
A:ICS502
|
2.2
|
68.2
|
1.0
|
|
S3B
|
A:ICS502
|
2.2
|
76.0
|
1.0
|
|
S1B
|
A:ICS502
|
2.2
|
65.9
|
1.0
|
|
FE2
|
A:ICS502
|
2.6
|
92.8
|
1.0
|
|
FE7
|
A:ICS502
|
2.6
|
70.1
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
79.6
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
80.2
|
1.0
|
|
FE3
|
A:ICS502
|
3.7
|
74.7
|
1.0
|
|
FE4
|
A:ICS502
|
3.7
|
80.9
|
1.0
|
|
S4B
|
A:ICS502
|
3.8
|
75.1
|
1.0
|
|
O7
|
A:HCA501
|
3.8
|
65.1
|
1.0
|
|
OE1
|
A:GLN207
|
4.1
|
70.3
|
1.0
|
|
CZ
|
A:PHE397
|
4.2
|
62.9
|
1.0
|
|
S2A
|
A:ICS502
|
4.2
|
72.4
|
1.0
|
|
S1A
|
A:ICS502
|
4.3
|
81.1
|
1.0
|
|
S5A
|
A:ICS502
|
4.5
|
62.6
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
62.3
|
1.0
|
|
CG2
|
A:VAL86
|
4.6
|
60.1
|
1.0
|
|
CE2
|
A:PHE397
|
5.0
|
62.0
|
1.0
|
|
FE1
|
A:ICS502
|
5.0
|
75.3
|
1.0
|
|
Iron binding site 7 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 7 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:70.1
occ:1.00
|
FE7
|
A:ICS502
|
0.0
|
70.1
|
1.0
|
|
CX
|
A:ICS502
|
2.0
|
78.7
|
1.0
|
|
S5A
|
A:ICS502
|
2.2
|
62.6
|
1.0
|
|
S4B
|
A:ICS502
|
2.2
|
75.1
|
1.0
|
|
S3B
|
A:ICS502
|
2.2
|
76.0
|
1.0
|
|
FE3
|
A:ICS502
|
2.6
|
74.7
|
1.0
|
|
FE6
|
A:ICS502
|
2.6
|
86.5
|
1.0
|
|
FE5
|
A:ICS502
|
2.6
|
79.6
|
1.0
|
|
MO1
|
A:ICS502
|
2.7
|
80.2
|
1.0
|
|
FE2
|
A:ICS502
|
3.7
|
92.8
|
1.0
|
|
FE4
|
A:ICS502
|
3.7
|
80.9
|
1.0
|
|
S1B
|
A:ICS502
|
3.8
|
65.9
|
1.0
|
|
S2A
|
A:ICS502
|
4.3
|
72.4
|
1.0
|
|
NH2
|
A:ARG112
|
4.3
|
63.0
|
1.0
|
|
S4A
|
A:ICS502
|
4.3
|
64.7
|
1.0
|
|
NE
|
A:ARG112
|
4.4
|
53.7
|
1.0
|
|
S2B
|
A:ICS502
|
4.4
|
68.2
|
1.0
|
|
CZ
|
A:ARG375
|
4.5
|
66.2
|
1.0
|
|
S3A
|
A:ICS502
|
4.5
|
62.3
|
1.0
|
|
NH2
|
A:ARG375
|
4.5
|
60.4
|
1.0
|
|
NH1
|
A:ARG375
|
4.7
|
66.8
|
1.0
|
|
O6
|
A:HCA501
|
4.7
|
72.9
|
1.0
|
|
O7
|
A:HCA501
|
4.8
|
65.1
|
1.0
|
|
NE
|
A:ARG375
|
4.8
|
68.7
|
1.0
|
|
CZ
|
A:ARG112
|
4.8
|
59.0
|
1.0
|
|
FE1
|
A:ICS502
|
5.0
|
75.3
|
1.0
|
|
Iron binding site 8 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 8 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:105.2
occ:1.00
|
FE1
|
B:CLF601
|
0.0
|
105.2
|
1.0
|
|
SG
|
A:CYS170
|
2.0
|
56.6
|
1.0
|
|
S2A
|
B:CLF601
|
2.3
|
98.1
|
1.0
|
|
S3A
|
B:CLF601
|
2.3
|
87.8
|
1.0
|
|
S1
|
B:CLF601
|
2.4
|
83.8
|
1.0
|
|
FE2
|
B:CLF601
|
2.5
|
116.9
|
1.0
|
|
FE4
|
B:CLF601
|
2.6
|
109.3
|
1.0
|
|
FE3
|
B:CLF601
|
2.8
|
106.6
|
1.0
|
|
CB
|
A:CYS170
|
3.0
|
50.7
|
1.0
|
|
CA
|
A:GLY201
|
3.8
|
57.8
|
1.0
|
|
S4A
|
B:CLF601
|
3.8
|
110.8
|
1.0
|
|
N
|
A:CYS170
|
3.8
|
57.1
|
1.0
|
|
CA
|
A:CYS170
|
3.9
|
54.2
|
1.0
|
|
SG
|
B:CYS94
|
4.0
|
59.2
|
1.0
|
|
N
|
A:GLY201
|
4.1
|
56.0
|
1.0
|
|
FE8
|
B:CLF601
|
4.4
|
102.8
|
1.0
|
|
OG
|
B:SER91
|
4.5
|
61.9
|
1.0
|
|
SG
|
A:CYS104
|
4.5
|
62.2
|
1.0
|
|
C
|
A:GLY201
|
4.6
|
58.6
|
1.0
|
|
FE5
|
B:CLF601
|
4.6
|
102.6
|
1.0
|
|
CB
|
B:SER91
|
4.6
|
56.6
|
1.0
|
|
N
|
A:PHE202
|
4.8
|
52.5
|
1.0
|
|
FE6
|
B:CLF601
|
4.9
|
98.9
|
1.0
|
|
C
|
A:GLU169
|
4.9
|
58.6
|
1.0
|
|
SG
|
A:CYS78
|
5.0
|
73.0
|
1.0
|
|
Iron binding site 9 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 9 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:116.9
occ:1.00
|
FE2
|
B:CLF601
|
0.0
|
116.9
|
1.0
|
|
SG
|
B:CYS94
|
2.2
|
59.2
|
1.0
|
|
S4A
|
B:CLF601
|
2.3
|
110.8
|
1.0
|
|
S2A
|
B:CLF601
|
2.3
|
98.1
|
1.0
|
|
S1
|
B:CLF601
|
2.5
|
83.8
|
1.0
|
|
FE1
|
B:CLF601
|
2.5
|
105.2
|
1.0
|
|
FE4
|
B:CLF601
|
2.6
|
109.3
|
1.0
|
|
FE3
|
B:CLF601
|
2.8
|
106.6
|
1.0
|
|
FE8
|
B:CLF601
|
2.9
|
102.8
|
1.0
|
|
N
|
B:CYS94
|
3.4
|
42.9
|
1.0
|
|
CB
|
B:CYS94
|
3.5
|
46.4
|
1.0
|
|
CA
|
B:CYS94
|
3.6
|
41.7
|
1.0
|
|
S3A
|
B:CLF601
|
3.8
|
87.8
|
1.0
|
|
FE5
|
B:CLF601
|
3.8
|
102.6
|
1.0
|
|
S4B
|
B:CLF601
|
3.9
|
100.1
|
1.0
|
|
C
|
B:GLY93
|
4.1
|
44.1
|
1.0
|
|
SG
|
A:CYS170
|
4.3
|
56.6
|
1.0
|
|
SG
|
A:CYS104
|
4.3
|
62.2
|
1.0
|
|
FE6
|
B:CLF601
|
4.6
|
98.9
|
1.0
|
|
CA
|
B:GLY93
|
4.7
|
42.9
|
1.0
|
|
CB
|
B:SER91
|
4.7
|
56.6
|
1.0
|
|
SG
|
A:CYS78
|
4.7
|
73.0
|
1.0
|
|
O
|
B:GLY93
|
4.8
|
43.9
|
1.0
|
|
Iron binding site 10 out
of 40 in 10zn
Go back to
Iron Binding Sites List in 10zn
Iron binding site 10 out
of 40 in the Cryoem Structure of Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry)
 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 Heterologous Nitrogenase Complex (2:1 A. Vinelandii-Fep:G. Diazotrophicus-Mofep) Inhibited By Befx (C2 Symmetry) within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe601
b:106.6
occ:1.00
|
FE3
|
B:CLF601
|
0.0
|
106.6
|
1.0
|
|
S4A
|
B:CLF601
|
2.3
|
110.8
|
1.0
|
|
S2A
|
B:CLF601
|
2.3
|
98.1
|
1.0
|
|
SG
|
A:CYS78
|
2.3
|
73.0
|
1.0
|
|
S3A
|
B:CLF601
|
2.3
|
87.8
|
1.0
|
|
FE4
|
B:CLF601
|
2.7
|
109.3
|
1.0
|
|
FE2
|
B:CLF601
|
2.8
|
116.9
|
1.0
|
|
FE1
|
B:CLF601
|
2.8
|
105.2
|
1.0
|
|
CB
|
A:CYS78
|
3.1
|
63.3
|
1.0
|
|
CA
|
A:GLY201
|
3.7
|
57.8
|
1.0
|
|
CB
|
A:TYR80
|
3.9
|
57.7
|
1.0
|
|
S1
|
B:CLF601
|
4.2
|
83.8
|
1.0
|
|
SG
|
A:CYS170
|
4.5
|
56.6
|
1.0
|
|
CD2
|
A:TYR80
|
4.5
|
53.4
|
1.0
|
|
N
|
A:GLY201
|
4.5
|
56.0
|
1.0
|
|
CG
|
A:TYR80
|
4.5
|
56.4
|
1.0
|
|
SG
|
A:CYS104
|
4.5
|
62.2
|
1.0
|
|
CA
|
A:CYS78
|
4.6
|
56.0
|
1.0
|
|
CA
|
B:GLY93
|
4.6
|
42.9
|
1.0
|
|
C
|
B:GLY93
|
4.7
|
44.1
|
1.0
|
|
N
|
B:CYS94
|
4.7
|
42.9
|
1.0
|
|
C
|
A:GLY201
|
4.8
|
58.6
|
1.0
|
|
N
|
A:TYR80
|
4.8
|
52.0
|
1.0
|
|
SG
|
B:CYS94
|
4.8
|
59.2
|
1.0
|
|
CA
|
A:TYR80
|
4.9
|
54.9
|
1.0
|
|
CE2
|
B:TYR97
|
4.9
|
41.8
|
1.0
|
|
Reference:
Y.Li,
S.M.Narehood,
B.D.Cook,
K.L.Mcguire,
M.A.Herzik Jr.,
F.A.Tezcan.
Structural and Functional Characterization of Heterologous Nitrogenase Complexes. Biochemistry 2026.
ISSN: ISSN 0006-2960
PubMed: 42390130
DOI: 10.1021/ACS.BIOCHEM.6C00360
Page generated: Sun Oct 4 08:33:19 2026
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