Iron in PDB 11my: Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
Enzymatic activity of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
All present enzymatic activity of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex:
1.18.6.1;
Other elements in 11my:
The structure of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex also contains other interesting chemical elements:
Iron Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
15;
Binding sites:
The binding sites of Iron atom in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
(pdb code 11my). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 15 binding sites of Iron where determined in the
Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex, PDB code: 11my:
Jump to Iron binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Iron binding site 1 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 1 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE1
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
S2A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
S4A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
S1A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
HG
|
C:CYS267
|
2.4
|
111.2
|
1.0
|
|
FE4
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE3
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE2
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
OG
|
C:SER270
|
2.7
|
122.5
|
1.0
|
|
SG
|
C:CYS267
|
2.7
|
116.6
|
1.0
|
|
HG
|
C:SER270
|
2.9
|
121.7
|
1.0
|
|
CX
|
C:ICS602
|
3.5
|
20.0
|
1.0
|
|
O
|
C:GLY350
|
3.9
|
133.6
|
1.0
|
|
CB
|
C:SER270
|
4.0
|
120.6
|
1.0
|
|
HB3
|
C:SER351
|
4.2
|
125.5
|
1.0
|
|
HB2
|
C:SER270
|
4.2
|
120.1
|
1.0
|
|
CB
|
C:CYS267
|
4.3
|
116.9
|
1.0
|
|
H
|
C:SER270
|
4.3
|
124.2
|
1.0
|
|
HB2
|
C:CYS267
|
4.3
|
117.5
|
1.0
|
|
HE1
|
C:TYR221
|
4.3
|
117.1
|
1.0
|
|
HB3
|
C:SER270
|
4.5
|
118.9
|
1.0
|
|
HB3
|
C:CYS267
|
4.7
|
116.3
|
1.0
|
|
S5A
|
C:ICS602
|
4.8
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
4.8
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
4.8
|
20.0
|
1.0
|
|
CE1
|
C:TYR221
|
4.9
|
116.8
|
1.0
|
|
C
|
C:GLY350
|
4.9
|
129.6
|
1.0
|
|
N
|
C:SER270
|
4.9
|
126.6
|
1.0
|
|
HH12
|
C:ARG92
|
4.9
|
103.3
|
1.0
|
|
HB3
|
C:ARG269
|
5.0
|
129.1
|
1.0
|
|
Iron binding site 2 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 2 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE2
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S2A
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S1A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
FE6
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE4
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE3
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
O
|
C:GLY350
|
2.9
|
133.6
|
1.0
|
|
H
|
C:GLY350
|
3.3
|
127.9
|
1.0
|
|
FE5
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
FE7
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
HB2
|
C:ARG352
|
3.8
|
120.5
|
1.0
|
|
S4A
|
C:ICS602
|
3.9
|
20.0
|
1.0
|
|
C
|
C:GLY350
|
4.0
|
129.6
|
1.0
|
|
N
|
C:GLY350
|
4.0
|
128.5
|
1.0
|
|
HD3
|
C:ARG352
|
4.1
|
115.7
|
1.0
|
|
S3B
|
C:ICS602
|
4.2
|
20.0
|
1.0
|
|
S1B
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
CA
|
C:GLY350
|
4.5
|
126.5
|
1.0
|
|
S3A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
S5A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
HA3
|
C:GLY350
|
4.6
|
128.6
|
1.0
|
|
HA3
|
C:GLY349
|
4.7
|
132.5
|
1.0
|
|
CB
|
C:ARG352
|
4.7
|
119.7
|
1.0
|
|
HB3
|
C:SER351
|
4.8
|
125.5
|
1.0
|
|
HH11
|
C:ARG352
|
4.9
|
114.8
|
1.0
|
|
CD
|
C:ARG352
|
4.9
|
113.2
|
1.0
|
|
Iron binding site 3 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 3 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE3
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S5A
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S4A
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S2A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
FE7
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE4
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE2
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
HG
|
C:SER270
|
3.4
|
121.7
|
1.0
|
|
FE6
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
FE5
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
S1A
|
C:ICS602
|
3.9
|
20.0
|
1.0
|
|
OG
|
C:SER270
|
3.9
|
122.5
|
1.0
|
|
HE2
|
C:HIS190
|
4.0
|
118.8
|
1.0
|
|
HG11
|
C:VAL66
|
4.1
|
104.4
|
1.0
|
|
HZ
|
C:PHE374
|
4.2
|
122.6
|
1.0
|
|
S4B
|
C:ICS602
|
4.2
|
20.0
|
1.0
|
|
S3B
|
C:ICS602
|
4.2
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
4.4
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
HG13
|
C:VAL66
|
4.6
|
105.3
|
1.0
|
|
NE2
|
C:HIS190
|
4.6
|
120.0
|
1.0
|
|
HE1
|
C:HIS190
|
4.6
|
113.2
|
1.0
|
|
HE1
|
C:PHE374
|
4.7
|
123.2
|
1.0
|
|
HH12
|
C:ARG92
|
4.7
|
103.3
|
1.0
|
|
HG
|
C:CYS267
|
4.7
|
111.2
|
1.0
|
|
O
|
C:GLY350
|
4.8
|
133.6
|
1.0
|
|
CG1
|
C:VAL66
|
4.8
|
104.4
|
1.0
|
|
H
|
C:GLY350
|
4.9
|
127.9
|
1.0
|
|
HH11
|
C:ARG92
|
4.9
|
113.8
|
1.0
|
|
CE1
|
C:HIS190
|
4.9
|
115.7
|
1.0
|
|
CZ
|
C:PHE374
|
5.0
|
120.7
|
1.0
|
|
Iron binding site 4 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 4 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE4
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S4A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
S1A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
FE5
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE3
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE2
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
FE1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
HH12
|
C:ARG92
|
3.2
|
103.3
|
1.0
|
|
FE7
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
FE6
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
S2A
|
C:ICS602
|
3.8
|
20.0
|
1.0
|
|
NH1
|
C:ARG92
|
3.9
|
107.7
|
1.0
|
|
HD11
|
C:ILE223
|
4.1
|
117.5
|
1.0
|
|
HH11
|
C:ARG92
|
4.1
|
113.8
|
1.0
|
|
S4B
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
HE
|
C:ARG92
|
4.3
|
127.0
|
1.0
|
|
S1B
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
HG
|
C:CYS267
|
4.4
|
111.2
|
1.0
|
|
HD12
|
C:ILE223
|
4.5
|
118.2
|
1.0
|
|
S5A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
HH12
|
C:ARG352
|
4.6
|
113.7
|
1.0
|
|
CD1
|
C:ILE223
|
4.6
|
119.2
|
1.0
|
|
HD13
|
C:ILE223
|
4.6
|
119.0
|
1.0
|
|
NH1
|
C:ARG352
|
4.6
|
114.5
|
1.0
|
|
HH11
|
C:ARG352
|
4.7
|
114.8
|
1.0
|
|
HD1
|
C:TYR221
|
4.7
|
116.9
|
1.0
|
|
OG
|
C:SER270
|
4.7
|
122.5
|
1.0
|
|
HG
|
C:SER270
|
4.7
|
121.7
|
1.0
|
|
CZ
|
C:ARG92
|
4.9
|
118.3
|
1.0
|
|
CD1
|
C:TYR221
|
4.9
|
116.7
|
1.0
|
|
HG13
|
C:VAL66
|
4.9
|
105.3
|
1.0
|
|
NE
|
C:ARG92
|
4.9
|
132.2
|
1.0
|
|
HE1
|
C:TYR221
|
5.0
|
117.1
|
1.0
|
|
Iron binding site 5 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 5 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE5
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S4B
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
S1B
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
FE6
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE4
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE7
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
MO1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
HB3
|
C:HIS485
|
3.6
|
111.0
|
1.0
|
|
HE
|
C:ARG92
|
3.7
|
127.0
|
1.0
|
|
FE2
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
FE3
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
S3B
|
C:ICS602
|
3.9
|
20.0
|
1.0
|
|
HD13
|
C:ILE223
|
3.9
|
119.0
|
1.0
|
|
HD11
|
C:ILE223
|
4.0
|
117.5
|
1.0
|
|
HH12
|
C:ARG92
|
4.1
|
103.3
|
1.0
|
|
S1A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
S4A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
CD1
|
C:ILE223
|
4.3
|
119.2
|
1.0
|
|
HG3
|
C:ARG92
|
4.4
|
118.6
|
1.0
|
|
S2B
|
C:ICS602
|
4.4
|
20.0
|
1.0
|
|
HA
|
C:HIS485
|
4.4
|
112.9
|
1.0
|
|
C5
|
C:HCA601
|
4.4
|
20.0
|
1.0
|
|
S5A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
O7
|
C:HCA601
|
4.5
|
20.0
|
1.0
|
|
CB
|
C:HIS485
|
4.5
|
115.4
|
1.0
|
|
NE
|
C:ARG92
|
4.5
|
132.2
|
1.0
|
|
HD12
|
C:ILE223
|
4.6
|
118.2
|
1.0
|
|
NH1
|
C:ARG92
|
4.6
|
107.7
|
1.0
|
|
HB2
|
C:HIS485
|
4.9
|
109.1
|
1.0
|
|
C6
|
C:HCA601
|
5.0
|
20.0
|
1.0
|
|
Iron binding site 6 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 6 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE6
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S3B
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S1B
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
FE7
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE2
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE5
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
MO1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
HB3
|
C:HIS485
|
3.2
|
111.0
|
1.0
|
|
FE3
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
HA3
|
C:GLY349
|
3.7
|
132.5
|
1.0
|
|
FE4
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
HD2
|
C:HIS485
|
3.8
|
99.7
|
1.0
|
|
S4B
|
C:ICS602
|
3.8
|
20.0
|
1.0
|
|
H
|
C:GLY349
|
3.8
|
129.1
|
1.0
|
|
H
|
C:GLY350
|
3.8
|
127.9
|
1.0
|
|
CD2
|
C:HIS485
|
4.1
|
96.8
|
1.0
|
|
CB
|
C:HIS485
|
4.1
|
115.4
|
1.0
|
|
CG
|
C:HIS485
|
4.2
|
108.9
|
1.0
|
|
S2A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
S1A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
O7
|
C:HCA601
|
4.4
|
20.0
|
1.0
|
|
HA
|
C:HIS485
|
4.4
|
112.9
|
1.0
|
|
N
|
C:GLY349
|
4.4
|
130.4
|
1.0
|
|
CA
|
C:GLY349
|
4.4
|
133.2
|
1.0
|
|
S5A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
HB1
|
C:ALA348
|
4.5
|
130.2
|
1.0
|
|
HB2
|
C:ARG352
|
4.6
|
120.5
|
1.0
|
|
N
|
C:GLY350
|
4.6
|
128.5
|
1.0
|
|
HB2
|
C:HIS485
|
4.7
|
109.1
|
1.0
|
|
CA
|
C:HIS485
|
4.8
|
118.3
|
1.0
|
|
O
|
C:GLY350
|
4.8
|
133.6
|
1.0
|
|
HZ
|
C:PHE374
|
4.9
|
122.6
|
1.0
|
|
NE2
|
C:HIS485
|
5.0
|
63.6
|
1.0
|
|
Iron binding site 7 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 7 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe602
b:20.0
occ:1.00
|
FE7
|
C:ICS602
|
0.0
|
20.0
|
1.0
|
|
CX
|
C:ICS602
|
2.0
|
20.0
|
1.0
|
|
S5A
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S4B
|
C:ICS602
|
2.2
|
20.0
|
1.0
|
|
S3B
|
C:ICS602
|
2.3
|
20.0
|
1.0
|
|
FE3
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE6
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
FE5
|
C:ICS602
|
2.6
|
20.0
|
1.0
|
|
MO1
|
C:ICS602
|
2.7
|
20.0
|
1.0
|
|
O7
|
C:HCA601
|
2.9
|
20.0
|
1.0
|
|
FE4
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
FE2
|
C:ICS602
|
3.7
|
20.0
|
1.0
|
|
S1B
|
C:ICS602
|
3.8
|
20.0
|
1.0
|
|
HZ
|
C:PHE374
|
4.0
|
122.6
|
1.0
|
|
O5
|
C:HCA601
|
4.0
|
20.0
|
1.0
|
|
C3
|
C:HCA601
|
4.2
|
20.0
|
1.0
|
|
S2A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
S4A
|
C:ICS602
|
4.3
|
20.0
|
1.0
|
|
S2B
|
C:ICS602
|
4.4
|
20.0
|
1.0
|
|
C5
|
C:HCA601
|
4.5
|
20.0
|
1.0
|
|
S3A
|
C:ICS602
|
4.5
|
20.0
|
1.0
|
|
HA3
|
C:GLY349
|
4.5
|
132.5
|
1.0
|
|
C7
|
C:HCA601
|
4.6
|
20.0
|
1.0
|
|
HB3
|
C:HIS485
|
4.6
|
111.0
|
1.0
|
|
C4
|
C:HCA601
|
4.8
|
20.0
|
1.0
|
|
HG22
|
C:VAL66
|
4.8
|
104.7
|
1.0
|
|
HG21
|
C:VAL66
|
4.9
|
104.2
|
1.0
|
|
CZ
|
C:PHE374
|
4.9
|
120.7
|
1.0
|
|
Iron binding site 8 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 8 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe601
b:193.4
occ:1.00
|
FE1
|
D:CLF601
|
0.0
|
193.4
|
1.0
|
|
S2A
|
D:CLF601
|
2.3
|
129.9
|
1.0
|
|
S3A
|
D:CLF601
|
2.3
|
174.0
|
1.0
|
|
S1
|
D:CLF601
|
2.4
|
217.7
|
1.0
|
|
FE2
|
D:CLF601
|
2.5
|
195.0
|
1.0
|
|
FE4
|
D:CLF601
|
2.6
|
201.5
|
1.0
|
|
FE3
|
D:CLF601
|
2.8
|
167.7
|
1.0
|
|
HA3
|
D:GLY47
|
2.9
|
127.7
|
1.0
|
|
HG
|
C:CYS58
|
3.2
|
118.8
|
1.0
|
|
N
|
D:CYS48
|
3.3
|
116.4
|
1.0
|
|
C
|
D:GLY47
|
3.4
|
121.4
|
1.0
|
|
CA
|
D:GLY47
|
3.6
|
129.9
|
1.0
|
|
HB2
|
C:CYS58
|
3.8
|
112.4
|
1.0
|
|
S4A
|
D:CLF601
|
3.8
|
192.4
|
1.0
|
|
CA
|
D:CYS48
|
4.0
|
116.4
|
1.0
|
|
O
|
D:GLY47
|
4.0
|
118.4
|
1.0
|
|
HG
|
C:CYS149
|
4.0
|
138.1
|
1.0
|
|
SG
|
C:CYS58
|
4.1
|
127.6
|
1.0
|
|
SG
|
C:CYS84
|
4.1
|
139.6
|
1.0
|
|
H
|
D:GLY47
|
4.2
|
126.2
|
1.0
|
|
CB
|
D:CYS48
|
4.2
|
114.5
|
1.0
|
|
HA2
|
D:GLY47
|
4.3
|
126.8
|
1.0
|
|
CB
|
C:CYS58
|
4.3
|
111.0
|
1.0
|
|
HB3
|
C:CYS58
|
4.3
|
110.6
|
1.0
|
|
FE8
|
D:CLF601
|
4.3
|
219.2
|
1.0
|
|
N
|
D:GLY47
|
4.4
|
125.2
|
1.0
|
|
HD2
|
D:TYR51
|
4.5
|
116.6
|
1.0
|
|
SG
|
C:CYS149
|
4.6
|
147.7
|
1.0
|
|
HG
|
D:SER45
|
4.6
|
132.1
|
1.0
|
|
SG
|
D:CYS48
|
4.6
|
133.0
|
1.0
|
|
FE5
|
D:CLF601
|
4.7
|
189.9
|
1.0
|
|
HE2
|
D:TYR51
|
4.8
|
115.1
|
1.0
|
|
OG
|
D:SER45
|
4.8
|
132.5
|
1.0
|
|
FE6
|
D:CLF601
|
4.9
|
209.7
|
1.0
|
|
Iron binding site 9 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 9 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe601
b:195.0
occ:1.00
|
FE2
|
D:CLF601
|
0.0
|
195.0
|
1.0
|
|
S4A
|
D:CLF601
|
2.3
|
192.4
|
1.0
|
|
SG
|
C:CYS84
|
2.3
|
139.6
|
1.0
|
|
S2A
|
D:CLF601
|
2.3
|
129.9
|
1.0
|
|
S1
|
D:CLF601
|
2.5
|
217.7
|
1.0
|
|
FE1
|
D:CLF601
|
2.5
|
193.4
|
1.0
|
|
FE4
|
D:CLF601
|
2.6
|
201.5
|
1.0
|
|
FE3
|
D:CLF601
|
2.7
|
167.7
|
1.0
|
|
FE8
|
D:CLF601
|
2.9
|
219.2
|
1.0
|
|
CB
|
C:CYS84
|
3.1
|
119.2
|
1.0
|
|
S3A
|
D:CLF601
|
3.8
|
174.0
|
1.0
|
|
FE5
|
D:CLF601
|
3.8
|
189.9
|
1.0
|
|
S4B
|
D:CLF601
|
3.9
|
175.0
|
1.0
|
|
CA
|
C:CYS84
|
4.0
|
107.1
|
1.0
|
|
HG22
|
C:THR148
|
4.0
|
123.7
|
1.0
|
|
HG21
|
C:THR148
|
4.2
|
122.0
|
1.0
|
|
HG23
|
C:THR148
|
4.3
|
120.5
|
1.0
|
|
HG
|
C:CYS149
|
4.4
|
138.1
|
1.0
|
|
CG2
|
C:THR148
|
4.4
|
124.1
|
1.0
|
|
SG
|
C:CYS149
|
4.5
|
147.7
|
1.0
|
|
HG
|
C:CYS58
|
4.5
|
118.8
|
1.0
|
|
FE6
|
D:CLF601
|
4.6
|
209.7
|
1.0
|
|
N
|
C:CYS84
|
4.7
|
104.0
|
1.0
|
|
H
|
C:CYS149
|
4.9
|
126.8
|
1.0
|
|
Iron binding site 10 out
of 15 in 11my
Go back to
Iron Binding Sites List in 11my
Iron binding site 10 out
of 15 in the Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex
 Mono view
 Stereo pair view
|
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe601
b:167.7
occ:1.00
|
FE3
|
D:CLF601
|
0.0
|
167.7
|
1.0
|
|
S4A
|
D:CLF601
|
2.3
|
192.4
|
1.0
|
|
S2A
|
D:CLF601
|
2.3
|
129.9
|
1.0
|
|
SG
|
C:CYS149
|
2.3
|
147.7
|
1.0
|
|
S3A
|
D:CLF601
|
2.3
|
174.0
|
1.0
|
|
HG
|
C:CYS149
|
2.5
|
138.1
|
1.0
|
|
HG
|
C:CYS58
|
2.5
|
118.8
|
1.0
|
|
FE4
|
D:CLF601
|
2.7
|
201.5
|
1.0
|
|
FE2
|
D:CLF601
|
2.7
|
195.0
|
1.0
|
|
FE1
|
D:CLF601
|
2.8
|
193.4
|
1.0
|
|
HA3
|
C:GLY180
|
3.0
|
131.7
|
1.0
|
|
H
|
C:CYS149
|
3.5
|
126.8
|
1.0
|
|
HG22
|
C:THR148
|
3.6
|
123.7
|
1.0
|
|
SG
|
C:CYS58
|
3.7
|
127.6
|
1.0
|
|
SG
|
C:CYS84
|
3.8
|
139.6
|
1.0
|
|
CB
|
C:CYS149
|
3.9
|
128.2
|
1.0
|
|
CA
|
C:GLY180
|
3.9
|
132.8
|
1.0
|
|
HB2
|
C:CYS149
|
4.0
|
127.2
|
1.0
|
|
HA2
|
C:GLY180
|
4.1
|
129.2
|
1.0
|
|
S1
|
D:CLF601
|
4.2
|
217.7
|
1.0
|
|
N
|
C:CYS149
|
4.2
|
126.5
|
1.0
|
|
HB3
|
C:PHE60
|
4.3
|
106.0
|
1.0
|
|
HG21
|
C:THR148
|
4.3
|
122.0
|
1.0
|
|
CG2
|
C:THR148
|
4.4
|
124.1
|
1.0
|
|
HB3
|
C:CYS149
|
4.5
|
127.0
|
1.0
|
|
HG
|
D:SER45
|
4.6
|
132.1
|
1.0
|
|
H
|
C:GLY180
|
4.6
|
131.2
|
1.0
|
|
C
|
C:GLY180
|
4.6
|
135.7
|
1.0
|
|
CA
|
C:CYS149
|
4.6
|
122.2
|
1.0
|
|
H
|
C:TYR181
|
4.6
|
132.3
|
1.0
|
|
HB2
|
C:PHE60
|
4.7
|
105.0
|
1.0
|
|
HG23
|
C:THR148
|
4.8
|
120.5
|
1.0
|
|
HA3
|
D:GLY47
|
4.8
|
127.7
|
1.0
|
|
N
|
C:GLY180
|
4.8
|
128.1
|
1.0
|
|
HA
|
C:THR148
|
4.8
|
118.9
|
1.0
|
|
HB3
|
C:CYS58
|
4.8
|
110.6
|
1.0
|
|
HA
|
C:CYS149
|
4.8
|
123.1
|
1.0
|
|
CB
|
C:CYS58
|
4.8
|
111.0
|
1.0
|
|
HB2
|
C:CYS58
|
4.9
|
112.4
|
1.0
|
|
N
|
C:TYR181
|
4.9
|
134.6
|
1.0
|
|
CB
|
C:PHE60
|
4.9
|
105.7
|
1.0
|
|
Reference:
R.Kashyap,
E.Antony.
Cryo-Em Structure of Trimeric Nitrogenase Mofe Protein From Methanosarcina Acetivorans Bound to the Nifi Inhibitor Complex To Be Published.
Page generated: Sun Oct 4 08:33:24 2026
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