Iron in PDB 6vxt: Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Enzymatic activity of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
All present enzymatic activity of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii:
1.18.6.1;
Protein crystallography data
The structure of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii, PDB code: 6vxt
was solved by
W.Kang,
Y.Hu,
M.W.Ribbe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
41.71 /
1.74
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
163.535,
203.435,
83.857,
90.00,
103.95,
90.00
|
R / Rfree (%)
|
17.2 /
20.3
|
Other elements in 6vxt:
The structure of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii also contains other interesting chemical elements:
Iron Binding Sites:
Iron binding site 1 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 1 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:33.8
occ:1.00
|
FE1
|
A:ICS602
|
0.0
|
33.8
|
1.0
|
S2A
|
A:ICS602
|
2.3
|
28.6
|
1.0
|
S4A
|
A:ICS602
|
2.3
|
31.4
|
1.0
|
S1A
|
A:ICS602
|
2.3
|
30.6
|
1.0
|
SG
|
A:CYS275
|
2.4
|
35.5
|
1.0
|
FE3
|
A:ICS602
|
2.6
|
31.5
|
1.0
|
FE2
|
A:ICS602
|
2.6
|
32.2
|
1.0
|
FE4
|
A:ICS602
|
2.7
|
31.4
|
1.0
|
CB
|
A:CYS275
|
3.3
|
30.2
|
1.0
|
CX
|
A:ICS602
|
3.4
|
27.1
|
1.0
|
OG
|
A:SER278
|
4.0
|
32.1
|
1.0
|
CB
|
A:LEU358
|
4.1
|
34.8
|
1.0
|
CB
|
A:SER278
|
4.4
|
34.1
|
1.0
|
CA
|
A:CYS275
|
4.5
|
33.8
|
1.0
|
CE2
|
A:TYR229
|
4.6
|
33.0
|
1.0
|
CD2
|
A:LEU358
|
4.7
|
36.3
|
1.0
|
S5A
|
A:ICS602
|
4.8
|
28.7
|
1.0
|
S2B
|
A:ICS602
|
4.8
|
31.9
|
1.0
|
S3A
|
A:ICS602
|
4.8
|
30.8
|
1.0
|
N
|
A:SER278
|
5.0
|
36.4
|
1.0
|
FE6
|
A:ICS602
|
5.0
|
30.5
|
1.0
|
FE5
|
A:ICS602
|
5.0
|
30.8
|
1.0
|
N
|
A:LEU358
|
5.0
|
33.5
|
1.0
|
CD2
|
A:TYR229
|
5.0
|
33.3
|
1.0
|
FE7
|
A:ICS602
|
5.0
|
31.6
|
1.0
|
|
Iron binding site 2 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 2 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:32.2
occ:1.00
|
FE2
|
A:ICS602
|
0.0
|
32.2
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S2A
|
A:ICS602
|
2.2
|
28.6
|
1.0
|
S2B
|
A:ICS602
|
2.2
|
31.9
|
1.0
|
S1A
|
A:ICS602
|
2.3
|
30.6
|
1.0
|
FE6
|
A:ICS602
|
2.6
|
30.5
|
1.0
|
FE4
|
A:ICS602
|
2.6
|
31.4
|
1.0
|
FE1
|
A:ICS602
|
2.6
|
33.8
|
1.0
|
FE3
|
A:ICS602
|
2.7
|
31.5
|
1.0
|
FE5
|
A:ICS602
|
3.6
|
30.8
|
1.0
|
FE7
|
A:ICS602
|
3.7
|
31.6
|
1.0
|
S4A
|
A:ICS602
|
3.8
|
31.4
|
1.0
|
NE2
|
A:HIS195
|
4.1
|
35.8
|
1.0
|
CZ
|
A:PHE381
|
4.1
|
33.0
|
1.0
|
S1B
|
A:ICS602
|
4.2
|
27.2
|
1.0
|
S3B
|
A:ICS602
|
4.2
|
31.0
|
1.0
|
CE1
|
A:HIS195
|
4.2
|
36.4
|
1.0
|
S3A
|
A:ICS602
|
4.4
|
30.8
|
1.0
|
S5A
|
A:ICS602
|
4.5
|
28.7
|
1.0
|
CE1
|
A:PHE381
|
4.5
|
31.6
|
1.0
|
CG1
|
A:VAL70
|
4.6
|
34.2
|
1.0
|
SG
|
A:CYS275
|
4.7
|
35.5
|
1.0
|
N
|
A:GLY357
|
4.9
|
35.7
|
1.0
|
|
Iron binding site 3 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 3 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:31.5
occ:1.00
|
FE3
|
A:ICS602
|
0.0
|
31.5
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S5A
|
A:ICS602
|
2.2
|
28.7
|
1.0
|
S4A
|
A:ICS602
|
2.2
|
31.4
|
1.0
|
S2A
|
A:ICS602
|
2.3
|
28.6
|
1.0
|
FE1
|
A:ICS602
|
2.6
|
33.8
|
1.0
|
FE2
|
A:ICS602
|
2.7
|
32.2
|
1.0
|
FE4
|
A:ICS602
|
2.7
|
31.4
|
1.0
|
FE7
|
A:ICS602
|
2.7
|
31.6
|
1.0
|
FE6
|
A:ICS602
|
3.7
|
30.5
|
1.0
|
FE5
|
A:ICS602
|
3.8
|
30.8
|
1.0
|
S1A
|
A:ICS602
|
3.8
|
30.6
|
1.0
|
NH2
|
A:ARG96
|
4.1
|
31.2
|
1.0
|
O
|
A:HOH906
|
4.1
|
34.8
|
1.0
|
CD2
|
A:TYR229
|
4.2
|
33.3
|
1.0
|
S3B
|
A:ICS602
|
4.3
|
31.0
|
1.0
|
S4B
|
A:ICS602
|
4.3
|
29.4
|
1.0
|
CE2
|
A:TYR229
|
4.5
|
33.0
|
1.0
|
S2B
|
A:ICS602
|
4.5
|
31.9
|
1.0
|
S3A
|
A:ICS602
|
4.6
|
30.8
|
1.0
|
SG
|
A:CYS275
|
4.9
|
35.5
|
1.0
|
|
Iron binding site 4 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 4 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:31.4
occ:1.00
|
FE4
|
A:ICS602
|
0.0
|
31.4
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S3A
|
A:ICS602
|
2.2
|
30.8
|
1.0
|
S4A
|
A:ICS602
|
2.3
|
31.4
|
1.0
|
S1A
|
A:ICS602
|
2.3
|
30.6
|
1.0
|
FE5
|
A:ICS602
|
2.6
|
30.8
|
1.0
|
FE2
|
A:ICS602
|
2.6
|
32.2
|
1.0
|
FE1
|
A:ICS602
|
2.7
|
33.8
|
1.0
|
FE3
|
A:ICS602
|
2.7
|
31.5
|
1.0
|
FE6
|
A:ICS602
|
3.7
|
30.5
|
1.0
|
FE7
|
A:ICS602
|
3.7
|
31.6
|
1.0
|
S2A
|
A:ICS602
|
3.8
|
28.6
|
1.0
|
N
|
A:GLY357
|
4.0
|
35.7
|
1.0
|
N
|
A:LEU358
|
4.0
|
33.5
|
1.0
|
CB
|
A:LEU358
|
4.0
|
34.8
|
1.0
|
S4B
|
A:ICS602
|
4.2
|
29.4
|
1.0
|
S1B
|
A:ICS602
|
4.3
|
27.2
|
1.0
|
S5A
|
A:ICS602
|
4.4
|
28.7
|
1.0
|
S2B
|
A:ICS602
|
4.5
|
31.9
|
1.0
|
N
|
A:ARG359
|
4.5
|
31.6
|
1.0
|
CA
|
A:LEU358
|
4.6
|
32.9
|
1.0
|
C
|
A:GLY357
|
4.6
|
38.2
|
1.0
|
CG
|
A:ARG359
|
4.6
|
29.7
|
1.0
|
CA
|
A:GLY357
|
4.6
|
31.7
|
1.0
|
SG
|
A:CYS275
|
4.7
|
35.5
|
1.0
|
CD
|
A:ARG359
|
4.8
|
31.5
|
1.0
|
CA
|
A:GLY356
|
4.8
|
35.0
|
1.0
|
C
|
A:GLY356
|
4.9
|
36.0
|
1.0
|
NE
|
A:ARG359
|
4.9
|
33.0
|
1.0
|
|
Iron binding site 5 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 5 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:30.8
occ:1.00
|
FE5
|
A:ICS602
|
0.0
|
30.8
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S1B
|
A:ICS602
|
2.2
|
27.2
|
1.0
|
S4B
|
A:ICS602
|
2.2
|
29.4
|
1.0
|
S3A
|
A:ICS602
|
2.3
|
30.8
|
1.0
|
FE6
|
A:ICS602
|
2.6
|
30.5
|
1.0
|
FE4
|
A:ICS602
|
2.6
|
31.4
|
1.0
|
FE7
|
A:ICS602
|
2.6
|
31.6
|
1.0
|
MO1
|
A:ICS602
|
2.7
|
32.2
|
1.0
|
FE2
|
A:ICS602
|
3.6
|
32.2
|
1.0
|
FE3
|
A:ICS602
|
3.8
|
31.5
|
1.0
|
ND1
|
A:HIS442
|
3.8
|
28.2
|
1.0
|
S3B
|
A:ICS602
|
3.8
|
31.0
|
1.0
|
N
|
A:GLY356
|
4.1
|
32.8
|
1.0
|
CA
|
A:GLY356
|
4.1
|
35.0
|
1.0
|
CE1
|
A:HIS442
|
4.2
|
33.4
|
1.0
|
CG2
|
A:ILE355
|
4.2
|
30.5
|
1.0
|
S1A
|
A:ICS602
|
4.3
|
30.6
|
1.0
|
S4A
|
A:ICS602
|
4.3
|
31.4
|
1.0
|
S2B
|
A:ICS602
|
4.4
|
31.9
|
1.0
|
S5A
|
A:ICS602
|
4.4
|
28.7
|
1.0
|
N
|
A:GLY357
|
4.6
|
35.7
|
1.0
|
CD
|
A:ARG359
|
4.7
|
31.5
|
1.0
|
O6
|
A:HCA601
|
4.7
|
24.4
|
1.0
|
O7
|
A:HCA601
|
4.8
|
35.8
|
1.0
|
CG
|
A:HIS442
|
4.8
|
31.8
|
1.0
|
C
|
A:GLY356
|
4.9
|
36.0
|
1.0
|
FE1
|
A:ICS602
|
5.0
|
33.8
|
1.0
|
|
Iron binding site 6 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 6 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:30.5
occ:1.00
|
FE6
|
A:ICS602
|
0.0
|
30.5
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S1B
|
A:ICS602
|
2.2
|
27.2
|
1.0
|
S2B
|
A:ICS602
|
2.2
|
31.9
|
1.0
|
S3B
|
A:ICS602
|
2.2
|
31.0
|
1.0
|
FE5
|
A:ICS602
|
2.6
|
30.8
|
1.0
|
FE7
|
A:ICS602
|
2.6
|
31.6
|
1.0
|
FE2
|
A:ICS602
|
2.6
|
32.2
|
1.0
|
MO1
|
A:ICS602
|
2.6
|
32.2
|
1.0
|
FE4
|
A:ICS602
|
3.7
|
31.4
|
1.0
|
FE3
|
A:ICS602
|
3.7
|
31.5
|
1.0
|
S4B
|
A:ICS602
|
3.8
|
29.4
|
1.0
|
O7
|
A:HCA601
|
3.8
|
35.8
|
1.0
|
CZ
|
A:PHE381
|
4.1
|
33.0
|
1.0
|
S2A
|
A:ICS602
|
4.2
|
28.6
|
1.0
|
S1A
|
A:ICS602
|
4.3
|
30.6
|
1.0
|
S5A
|
A:ICS602
|
4.4
|
28.7
|
1.0
|
S3A
|
A:ICS602
|
4.5
|
30.8
|
1.0
|
O6
|
A:HCA601
|
4.5
|
24.4
|
1.0
|
CG2
|
A:VAL70
|
4.5
|
29.2
|
1.0
|
O2
|
A:HCA601
|
4.6
|
31.1
|
1.0
|
ND1
|
A:HIS442
|
4.7
|
28.2
|
1.0
|
CE2
|
A:PHE381
|
4.7
|
32.5
|
1.0
|
C3
|
A:HCA601
|
4.8
|
36.5
|
1.0
|
FE1
|
A:ICS602
|
5.0
|
33.8
|
1.0
|
C2
|
A:HCA601
|
5.0
|
32.7
|
1.0
|
|
Iron binding site 7 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 7 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe602
b:31.6
occ:1.00
|
FE7
|
A:ICS602
|
0.0
|
31.6
|
1.0
|
CX
|
A:ICS602
|
2.0
|
27.1
|
1.0
|
S5A
|
A:ICS602
|
2.2
|
28.7
|
1.0
|
S4B
|
A:ICS602
|
2.2
|
29.4
|
1.0
|
S3B
|
A:ICS602
|
2.2
|
31.0
|
1.0
|
FE6
|
A:ICS602
|
2.6
|
30.5
|
1.0
|
FE5
|
A:ICS602
|
2.6
|
30.8
|
1.0
|
MO1
|
A:ICS602
|
2.6
|
32.2
|
1.0
|
FE3
|
A:ICS602
|
2.7
|
31.5
|
1.0
|
FE4
|
A:ICS602
|
3.7
|
31.4
|
1.0
|
FE2
|
A:ICS602
|
3.7
|
32.2
|
1.0
|
O6
|
A:HCA601
|
3.7
|
24.4
|
1.0
|
S1B
|
A:ICS602
|
3.8
|
27.2
|
1.0
|
O
|
A:HOH876
|
3.8
|
32.6
|
1.0
|
NE
|
A:ARG96
|
4.2
|
32.0
|
1.0
|
S2A
|
A:ICS602
|
4.3
|
28.6
|
1.0
|
NH2
|
A:ARG96
|
4.3
|
31.2
|
1.0
|
S4A
|
A:ICS602
|
4.3
|
31.4
|
1.0
|
S2B
|
A:ICS602
|
4.4
|
31.9
|
1.0
|
S3A
|
A:ICS602
|
4.5
|
30.8
|
1.0
|
C7
|
A:HCA601
|
4.7
|
31.8
|
1.0
|
ND1
|
A:HIS442
|
4.7
|
28.2
|
1.0
|
O7
|
A:HCA601
|
4.7
|
35.8
|
1.0
|
CZ
|
A:ARG96
|
4.8
|
31.9
|
1.0
|
CZ
|
A:ARG359
|
4.8
|
32.9
|
1.0
|
NH1
|
A:ARG359
|
4.8
|
32.3
|
1.0
|
FE1
|
A:ICS602
|
5.0
|
33.8
|
1.0
|
|
Iron binding site 8 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 8 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe608
b:33.0
occ:1.00
|
FE1
|
A:CLF608
|
0.0
|
33.0
|
1.0
|
S3A
|
A:CLF608
|
2.3
|
32.0
|
1.0
|
S2A
|
A:CLF608
|
2.3
|
34.2
|
1.0
|
S1
|
A:CLF608
|
2.4
|
32.6
|
1.0
|
SG
|
A:CYS154
|
2.4
|
32.4
|
1.0
|
FE2
|
A:CLF608
|
2.5
|
32.9
|
1.0
|
FE4
|
A:CLF608
|
2.5
|
32.5
|
1.0
|
FE3
|
A:CLF608
|
2.7
|
32.0
|
1.0
|
CB
|
A:CYS154
|
3.3
|
34.4
|
1.0
|
S4A
|
A:CLF608
|
3.8
|
32.2
|
1.0
|
O
|
B:HOH739
|
3.8
|
33.4
|
1.0
|
N
|
A:CYS154
|
3.9
|
34.6
|
1.0
|
CA
|
A:GLY185
|
3.9
|
35.9
|
1.0
|
OG
|
B:SER92
|
4.0
|
34.3
|
0.5
|
N
|
A:GLY185
|
4.1
|
37.1
|
1.0
|
CA
|
A:CYS154
|
4.2
|
31.1
|
1.0
|
SG
|
B:CYS95
|
4.2
|
32.3
|
1.0
|
FE8
|
A:CLF608
|
4.4
|
33.5
|
1.0
|
FE5
|
A:CLF608
|
4.5
|
32.5
|
1.0
|
SG
|
A:CYS88
|
4.6
|
35.1
|
1.0
|
C
|
A:GLY185
|
4.7
|
36.5
|
1.0
|
CB
|
B:SER92
|
4.8
|
42.0
|
1.0
|
FE6
|
A:CLF608
|
4.8
|
35.5
|
1.0
|
SG
|
A:CYS62
|
4.9
|
31.7
|
1.0
|
SG
|
B:CYS153
|
5.0
|
35.3
|
1.0
|
|
Iron binding site 9 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 9 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe608
b:32.9
occ:1.00
|
FE2
|
A:CLF608
|
0.0
|
32.9
|
1.0
|
S2A
|
A:CLF608
|
2.3
|
34.2
|
1.0
|
S4A
|
A:CLF608
|
2.3
|
32.2
|
1.0
|
SG
|
B:CYS95
|
2.4
|
32.3
|
1.0
|
FE1
|
A:CLF608
|
2.5
|
33.0
|
1.0
|
S1
|
A:CLF608
|
2.5
|
32.6
|
1.0
|
FE4
|
A:CLF608
|
2.5
|
32.5
|
1.0
|
FE3
|
A:CLF608
|
2.7
|
32.0
|
1.0
|
FE8
|
A:CLF608
|
3.0
|
33.5
|
1.0
|
N
|
B:CYS95
|
3.3
|
37.9
|
1.0
|
CA
|
B:CYS95
|
3.6
|
28.8
|
1.0
|
CB
|
B:CYS95
|
3.6
|
26.3
|
1.0
|
FE5
|
A:CLF608
|
3.7
|
32.5
|
1.0
|
S3A
|
A:CLF608
|
3.8
|
32.0
|
1.0
|
C
|
B:GLY94
|
3.9
|
33.3
|
1.0
|
S4B
|
A:CLF608
|
3.9
|
29.1
|
1.0
|
OG
|
B:SER92
|
4.2
|
34.3
|
0.5
|
CA
|
B:GLY94
|
4.4
|
32.4
|
1.0
|
O
|
B:HOH739
|
4.4
|
33.4
|
1.0
|
SG
|
A:CYS88
|
4.6
|
35.1
|
1.0
|
FE6
|
A:CLF608
|
4.6
|
35.5
|
1.0
|
SG
|
A:CYS154
|
4.6
|
32.4
|
1.0
|
O
|
B:GLY94
|
4.6
|
32.8
|
1.0
|
SG
|
A:CYS62
|
4.8
|
31.7
|
1.0
|
N
|
B:GLY94
|
4.8
|
32.5
|
1.0
|
|
Iron binding site 10 out
of 32 in 6vxt
Go back to
Iron Binding Sites List in 6vxt
Iron binding site 10 out
of 32 in the Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Activated Nitrogenase Mofe-Protein From Azotobacter Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe608
b:32.0
occ:1.00
|
FE3
|
A:CLF608
|
0.0
|
32.0
|
1.0
|
S4A
|
A:CLF608
|
2.3
|
32.2
|
1.0
|
S2A
|
A:CLF608
|
2.3
|
34.2
|
1.0
|
S3A
|
A:CLF608
|
2.3
|
32.0
|
1.0
|
SG
|
A:CYS62
|
2.4
|
31.7
|
1.0
|
FE4
|
A:CLF608
|
2.6
|
32.5
|
1.0
|
FE2
|
A:CLF608
|
2.7
|
32.9
|
1.0
|
FE1
|
A:CLF608
|
2.7
|
33.0
|
1.0
|
CB
|
A:CYS62
|
3.4
|
31.1
|
1.0
|
CA
|
A:GLY185
|
3.9
|
35.9
|
1.0
|
CB
|
A:TYR64
|
4.1
|
28.6
|
1.0
|
S1
|
A:CLF608
|
4.2
|
32.6
|
1.0
|
CA
|
B:GLY94
|
4.2
|
32.4
|
1.0
|
C
|
B:GLY94
|
4.5
|
33.3
|
1.0
|
N
|
A:GLY185
|
4.5
|
37.1
|
1.0
|
CD1
|
A:TYR64
|
4.6
|
36.0
|
1.0
|
CG
|
A:TYR64
|
4.6
|
33.6
|
1.0
|
N
|
B:CYS95
|
4.6
|
37.9
|
1.0
|
SG
|
A:CYS154
|
4.8
|
32.4
|
1.0
|
CA
|
A:CYS62
|
4.8
|
30.2
|
1.0
|
O
|
B:HOH970
|
4.8
|
34.3
|
1.0
|
SG
|
A:CYS88
|
4.9
|
35.1
|
1.0
|
N
|
A:TYR64
|
4.9
|
34.4
|
1.0
|
N
|
B:GLY94
|
5.0
|
32.5
|
1.0
|
CE2
|
B:TYR98
|
5.0
|
34.2
|
1.0
|
C
|
A:GLY185
|
5.0
|
36.5
|
1.0
|
|
Reference:
W.Kang,
C.C.Lee,
A.J.Jasniewski,
M.W.Ribbe,
Y.Hu.
Structural Evidence For A Dynamic Metallocofactor During N Reduction By Mo-Nitrogenase Science 2020.
ISSN: ESSN 1095-9203
DOI: 10.1126/SCIENCE.AAZ6748
Page generated: Wed Aug 7 13:39:21 2024
|