Iron in PDB 5bvh: Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Enzymatic activity of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
All present enzymatic activity of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii:
1.18.6.1;
Protein crystallography data
The structure of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii, PDB code: 5bvh
was solved by
T.Spatzal,
K.A.Perez,
J.B.Howard,
D.C.Rees,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
100.43 /
1.53
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
81.071,
130.833,
107.318,
90.00,
110.64,
90.00
|
R / Rfree (%)
|
14.4 /
16
|
Other elements in 5bvh:
The structure of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii also contains other interesting chemical elements:
Iron Binding Sites:
Iron binding site 1 out
of 46 in 5bvh
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Iron Binding Sites List in 5bvh
Iron binding site 1 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:9.1
occ:0.65
|
FE1
|
A:ICS502
|
0.0
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
0.0
|
9.1
|
0.3
|
S2A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
SG
|
A:CYS275
|
2.3
|
8.4
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
2.3
|
9.4
|
0.3
|
S1A
|
A:ICS502
|
2.3
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
2.3
|
8.7
|
0.3
|
FE2
|
A:ICS502
|
2.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.6
|
8.5
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE3
|
A:ICS502
|
2.7
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.7
|
8.6
|
0.3
|
CB
|
A:CYS275
|
3.3
|
8.8
|
1.0
|
CX
|
A:ICS502
|
3.4
|
8.4
|
0.7
|
CX
|
A:ICH503
|
3.4
|
8.4
|
0.3
|
OG
|
A:SER278
|
4.0
|
9.3
|
1.0
|
CB
|
A:LEU358
|
4.2
|
9.2
|
1.0
|
CB
|
A:SER278
|
4.4
|
9.6
|
1.0
|
CE2
|
A:TYR229
|
4.5
|
9.2
|
1.0
|
CA
|
A:CYS275
|
4.5
|
9.3
|
1.0
|
C
|
A:CMO506
|
4.5
|
7.6
|
0.9
|
CD2
|
A:LEU358
|
4.7
|
9.1
|
1.0
|
SE2B
|
A:ICH503
|
4.8
|
4.2
|
0.1
|
S5A
|
A:ICS502
|
4.9
|
7.8
|
0.6
|
S3A
|
A:ICS502
|
4.9
|
7.6
|
0.7
|
N
|
A:SER278
|
4.9
|
9.4
|
1.0
|
SE3A
|
A:ICH503
|
4.9
|
9.5
|
0.3
|
FE6
|
A:ICS502
|
4.9
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
4.9
|
8.9
|
0.3
|
CD2
|
A:TYR229
|
4.9
|
9.3
|
1.0
|
SE5A
|
A:ICH503
|
4.9
|
10.5
|
0.4
|
N
|
A:LEU358
|
5.0
|
9.2
|
1.0
|
FE7
|
A:ICS502
|
5.0
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
5.0
|
8.6
|
0.3
|
|
Iron binding site 2 out
of 46 in 5bvh
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Iron Binding Sites List in 5bvh
Iron binding site 2 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.5
occ:0.65
|
FE2
|
A:ICS502
|
0.0
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
0.0
|
8.5
|
0.3
|
C
|
A:CMO506
|
1.9
|
7.6
|
0.9
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S2A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
S1A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
SE2B
|
A:ICH503
|
2.3
|
4.2
|
0.1
|
FE6
|
A:ICS502
|
2.5
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
2.5
|
8.9
|
0.3
|
FE1
|
A:ICS502
|
2.6
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
2.6
|
9.1
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE3
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
O
|
A:CMO506
|
2.9
|
8.2
|
0.9
|
FE7
|
A:ICS502
|
3.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
3.6
|
8.6
|
0.3
|
FE5
|
A:ICS502
|
3.6
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
3.6
|
8.7
|
0.3
|
S4A
|
A:ICS502
|
3.8
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
3.8
|
9.4
|
0.3
|
CZ
|
A:PHE381
|
4.0
|
8.6
|
1.0
|
S1B
|
A:ICS502
|
4.1
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
4.1
|
8.3
|
0.3
|
S3B
|
A:ICS502
|
4.1
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
4.1
|
8.4
|
0.3
|
NE2
|
A:HIS195
|
4.2
|
10.8
|
1.0
|
CE1
|
A:HIS195
|
4.4
|
10.8
|
1.0
|
CG1
|
A:VAL70
|
4.4
|
10.4
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
7.8
|
0.6
|
S3A
|
A:ICS502
|
4.5
|
7.6
|
0.7
|
CE1
|
A:PHE381
|
4.5
|
8.6
|
1.0
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
SE5A
|
A:ICH503
|
4.6
|
10.5
|
0.4
|
SG
|
A:CYS275
|
4.6
|
8.4
|
1.0
|
MO1
|
A:ICS502
|
4.9
|
8.1
|
0.7
|
MO1
|
A:ICH503
|
4.9
|
8.1
|
0.3
|
CG2
|
A:VAL70
|
5.0
|
10.4
|
1.0
|
N
|
A:GLY357
|
5.0
|
8.6
|
1.0
|
|
Iron binding site 3 out
of 46 in 5bvh
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Iron Binding Sites List in 5bvh
Iron binding site 3 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.6
occ:0.65
|
FE3
|
A:ICS502
|
0.0
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
0.0
|
8.6
|
0.3
|
CX
|
A:ICS502
|
1.9
|
8.4
|
0.7
|
CX
|
A:ICH503
|
1.9
|
8.4
|
0.3
|
S4A
|
A:ICS502
|
2.2
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
2.2
|
9.4
|
0.3
|
S5A
|
A:ICS502
|
2.2
|
7.8
|
0.6
|
S2A
|
A:ICS502
|
2.3
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.3
|
8.7
|
0.3
|
SE5A
|
A:ICH503
|
2.3
|
10.5
|
0.4
|
FE7
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE2
|
A:ICS502
|
2.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.6
|
8.5
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE1
|
A:ICS502
|
2.7
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
2.7
|
9.1
|
0.3
|
FE6
|
A:ICS502
|
3.7
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
3.7
|
8.9
|
0.3
|
FE5
|
A:ICS502
|
3.7
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
3.7
|
8.7
|
0.3
|
S1A
|
A:ICS502
|
3.9
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
3.9
|
8.7
|
0.3
|
O
|
A:HOH921
|
4.1
|
9.4
|
1.0
|
NH2
|
A:ARG96
|
4.1
|
9.6
|
1.0
|
CD2
|
A:TYR229
|
4.1
|
9.3
|
1.0
|
C
|
A:CMO506
|
4.1
|
7.6
|
0.9
|
S3B
|
A:ICS502
|
4.2
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
4.2
|
8.4
|
0.3
|
S4B
|
A:ICS502
|
4.3
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
4.3
|
8.5
|
0.3
|
CE2
|
A:TYR229
|
4.5
|
9.2
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
7.6
|
0.7
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
SE2B
|
A:ICH503
|
4.6
|
4.2
|
0.1
|
SG
|
A:CYS275
|
4.8
|
8.4
|
1.0
|
|
Iron binding site 4 out
of 46 in 5bvh
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Iron Binding Sites List in 5bvh
Iron binding site 4 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.7
occ:0.65
|
FE4
|
A:ICS502
|
0.0
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
0.0
|
8.7
|
0.3
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S3A
|
A:ICS502
|
2.3
|
7.6
|
0.7
|
S4A
|
A:ICS502
|
2.3
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
2.3
|
9.4
|
0.3
|
S1A
|
A:ICS502
|
2.3
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
2.3
|
8.7
|
0.3
|
SE3A
|
A:ICH503
|
2.3
|
9.5
|
0.3
|
FE2
|
A:ICS502
|
2.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.6
|
8.5
|
0.3
|
FE3
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE5
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE1
|
A:ICS502
|
2.6
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
2.6
|
9.1
|
0.3
|
FE6
|
A:ICS502
|
3.7
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
3.7
|
8.9
|
0.3
|
FE7
|
A:ICS502
|
3.7
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
3.7
|
8.6
|
0.3
|
S2A
|
A:ICS502
|
3.8
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
3.8
|
8.7
|
0.3
|
N
|
A:LEU358
|
4.0
|
9.2
|
1.0
|
CB
|
A:LEU358
|
4.0
|
9.2
|
1.0
|
N
|
A:GLY357
|
4.0
|
8.6
|
1.0
|
C
|
A:CMO506
|
4.2
|
7.6
|
0.9
|
S1B
|
A:ICS502
|
4.3
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
4.3
|
8.3
|
0.3
|
S4B
|
A:ICS502
|
4.3
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
4.3
|
8.5
|
0.3
|
S5A
|
A:ICS502
|
4.5
|
7.8
|
0.6
|
SE5A
|
A:ICH503
|
4.6
|
10.5
|
0.4
|
CA
|
A:LEU358
|
4.6
|
9.0
|
1.0
|
C
|
A:GLY357
|
4.6
|
9.1
|
1.0
|
N
|
A:ARG359
|
4.6
|
8.7
|
1.0
|
SG
|
A:CYS275
|
4.6
|
8.4
|
1.0
|
SE2B
|
A:ICH503
|
4.6
|
4.2
|
0.1
|
CA
|
A:GLY357
|
4.6
|
8.8
|
1.0
|
CG
|
A:ARG359
|
4.8
|
8.5
|
1.0
|
CD
|
A:ARG359
|
4.9
|
8.2
|
1.0
|
CA
|
A:GLY356
|
4.9
|
8.5
|
1.0
|
C
|
A:GLY356
|
5.0
|
8.4
|
1.0
|
|
Iron binding site 5 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 5 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 5 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.7
occ:0.65
|
FE5
|
A:ICS502
|
0.0
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
0.0
|
8.7
|
0.3
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S4B
|
A:ICS502
|
2.2
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
2.2
|
8.5
|
0.3
|
S1B
|
A:ICS502
|
2.3
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
2.3
|
8.3
|
0.3
|
S3A
|
A:ICS502
|
2.3
|
7.6
|
0.7
|
SE3A
|
A:ICH503
|
2.3
|
9.5
|
0.3
|
FE6
|
A:ICS502
|
2.6
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
2.6
|
8.9
|
0.3
|
FE7
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
MO1
|
A:ICS502
|
2.7
|
8.1
|
0.7
|
MO1
|
A:ICH503
|
2.7
|
8.1
|
0.3
|
FE2
|
A:ICS502
|
3.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
3.6
|
8.5
|
0.3
|
FE3
|
A:ICS502
|
3.7
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
3.7
|
8.6
|
0.3
|
ND1
|
A:HIS442
|
3.8
|
8.0
|
1.0
|
S3B
|
A:ICS502
|
3.9
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
3.9
|
8.4
|
0.3
|
C
|
A:CMO506
|
4.1
|
7.6
|
0.9
|
N
|
A:GLY356
|
4.1
|
8.4
|
1.0
|
CG2
|
A:ILE355
|
4.2
|
9.1
|
1.0
|
CA
|
A:GLY356
|
4.2
|
8.5
|
1.0
|
CE1
|
A:HIS442
|
4.2
|
8.0
|
1.0
|
S1A
|
A:ICS502
|
4.3
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
4.3
|
8.7
|
0.3
|
S4A
|
A:ICS502
|
4.4
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
4.4
|
9.4
|
0.3
|
S5A
|
A:ICS502
|
4.5
|
7.8
|
0.6
|
SE5A
|
A:ICH503
|
4.5
|
10.5
|
0.4
|
SE2B
|
A:ICH503
|
4.6
|
4.2
|
0.1
|
CG
|
A:HIS442
|
4.7
|
8.0
|
1.0
|
O6
|
A:HCA501
|
4.7
|
8.5
|
1.0
|
O7
|
A:HCA501
|
4.7
|
8.7
|
1.0
|
CD
|
A:ARG359
|
4.7
|
8.2
|
1.0
|
N
|
A:GLY357
|
4.7
|
8.6
|
1.0
|
|
Iron binding site 6 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 6 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 6 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.9
occ:0.65
|
FE6
|
A:ICS502
|
0.0
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
0.0
|
8.9
|
0.3
|
C
|
A:CMO506
|
1.9
|
7.6
|
0.9
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S1B
|
A:ICS502
|
2.2
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
2.2
|
8.3
|
0.3
|
S3B
|
A:ICS502
|
2.2
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
2.2
|
8.4
|
0.3
|
SE2B
|
A:ICH503
|
2.3
|
4.2
|
0.1
|
FE2
|
A:ICS502
|
2.5
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.5
|
8.5
|
0.3
|
FE7
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE5
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
MO1
|
A:ICS502
|
2.6
|
8.1
|
0.7
|
MO1
|
A:ICH503
|
2.6
|
8.1
|
0.3
|
O
|
A:CMO506
|
2.8
|
8.2
|
0.9
|
FE3
|
A:ICS502
|
3.7
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
3.7
|
8.6
|
0.3
|
FE4
|
A:ICS502
|
3.7
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
3.7
|
8.7
|
0.3
|
S4B
|
A:ICS502
|
3.8
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
3.8
|
8.5
|
0.3
|
O7
|
A:HCA501
|
3.8
|
8.7
|
1.0
|
CZ
|
A:PHE381
|
4.1
|
8.6
|
1.0
|
S2A
|
A:ICS502
|
4.1
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
4.1
|
8.7
|
0.3
|
S1A
|
A:ICS502
|
4.2
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
4.2
|
8.7
|
0.3
|
CG2
|
A:VAL70
|
4.4
|
10.4
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
7.8
|
0.6
|
O6
|
A:HCA501
|
4.5
|
8.5
|
1.0
|
SE5A
|
A:ICH503
|
4.5
|
10.5
|
0.4
|
S3A
|
A:ICS502
|
4.5
|
7.6
|
0.7
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
CE2
|
A:PHE381
|
4.6
|
8.8
|
1.0
|
O2
|
A:HCA501
|
4.6
|
10.3
|
1.0
|
ND1
|
A:HIS442
|
4.7
|
8.0
|
1.0
|
C3
|
A:HCA501
|
4.8
|
8.7
|
1.0
|
FE1
|
A:ICS502
|
4.9
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
4.9
|
9.1
|
0.3
|
|
Iron binding site 7 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 7 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 7 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe502
b:8.6
occ:0.65
|
FE7
|
A:ICS502
|
0.0
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
0.0
|
8.6
|
0.3
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S5A
|
A:ICS502
|
2.2
|
7.8
|
0.6
|
S3B
|
A:ICS502
|
2.2
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
2.2
|
8.4
|
0.3
|
S4B
|
A:ICS502
|
2.3
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
2.3
|
8.5
|
0.3
|
SE5A
|
A:ICH503
|
2.3
|
10.5
|
0.4
|
FE6
|
A:ICS502
|
2.6
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
2.6
|
8.9
|
0.3
|
FE3
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE5
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
MO1
|
A:ICS502
|
2.7
|
8.1
|
0.7
|
MO1
|
A:ICH503
|
2.7
|
8.1
|
0.3
|
FE2
|
A:ICS502
|
3.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
3.6
|
8.5
|
0.3
|
O
|
A:HOH820
|
3.7
|
9.4
|
1.0
|
FE4
|
A:ICS502
|
3.7
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
3.7
|
8.7
|
0.3
|
O6
|
A:HCA501
|
3.7
|
8.5
|
1.0
|
S1B
|
A:ICS502
|
3.8
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
3.8
|
8.3
|
0.3
|
C
|
A:CMO506
|
4.1
|
7.6
|
0.9
|
NE
|
A:ARG96
|
4.1
|
9.8
|
1.0
|
S2A
|
A:ICS502
|
4.2
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
4.2
|
8.7
|
0.3
|
NH2
|
A:ARG96
|
4.2
|
9.6
|
1.0
|
S4A
|
A:ICS502
|
4.3
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
4.3
|
9.4
|
0.3
|
S3A
|
A:ICS502
|
4.6
|
7.6
|
0.7
|
SE2B
|
A:ICH503
|
4.6
|
4.2
|
0.1
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
O7
|
A:HCA501
|
4.7
|
8.7
|
1.0
|
C7
|
A:HCA501
|
4.7
|
8.6
|
1.0
|
CZ
|
A:ARG96
|
4.7
|
9.6
|
1.0
|
ND1
|
A:HIS442
|
4.7
|
8.0
|
1.0
|
NH1
|
A:ARG359
|
4.8
|
8.2
|
1.0
|
CZ
|
A:ARG359
|
4.8
|
8.3
|
1.0
|
FE1
|
A:ICS502
|
5.0
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
5.0
|
9.1
|
0.3
|
|
Iron binding site 8 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 8 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 8 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe503
b:9.1
occ:0.35
|
FE1
|
A:ICS502
|
0.0
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
0.0
|
9.1
|
0.3
|
S2A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
SG
|
A:CYS275
|
2.3
|
8.4
|
1.0
|
S4A
|
A:ICS502
|
2.3
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
2.3
|
9.4
|
0.3
|
S1A
|
A:ICS502
|
2.3
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
2.3
|
8.7
|
0.3
|
FE2
|
A:ICS502
|
2.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.6
|
8.5
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE3
|
A:ICS502
|
2.7
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.7
|
8.6
|
0.3
|
CB
|
A:CYS275
|
3.3
|
8.8
|
1.0
|
CX
|
A:ICS502
|
3.4
|
8.4
|
0.7
|
CX
|
A:ICH503
|
3.4
|
8.4
|
0.3
|
OG
|
A:SER278
|
4.0
|
9.3
|
1.0
|
CB
|
A:LEU358
|
4.2
|
9.2
|
1.0
|
CB
|
A:SER278
|
4.4
|
9.6
|
1.0
|
CE2
|
A:TYR229
|
4.5
|
9.2
|
1.0
|
CA
|
A:CYS275
|
4.5
|
9.3
|
1.0
|
C
|
A:CMO506
|
4.5
|
7.6
|
0.9
|
CD2
|
A:LEU358
|
4.7
|
9.1
|
1.0
|
SE2B
|
A:ICH503
|
4.8
|
4.2
|
0.1
|
S5A
|
A:ICS502
|
4.9
|
7.8
|
0.6
|
S3A
|
A:ICS502
|
4.9
|
7.6
|
0.7
|
N
|
A:SER278
|
4.9
|
9.4
|
1.0
|
SE3A
|
A:ICH503
|
4.9
|
9.5
|
0.3
|
FE6
|
A:ICS502
|
4.9
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
4.9
|
8.9
|
0.3
|
CD2
|
A:TYR229
|
4.9
|
9.3
|
1.0
|
SE5A
|
A:ICH503
|
4.9
|
10.5
|
0.4
|
N
|
A:LEU358
|
5.0
|
9.2
|
1.0
|
FE7
|
A:ICS502
|
5.0
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
5.0
|
8.6
|
0.3
|
|
Iron binding site 9 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 9 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 9 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe503
b:8.6
occ:0.35
|
FE3
|
A:ICS502
|
0.0
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
0.0
|
8.6
|
0.3
|
CX
|
A:ICS502
|
1.9
|
8.4
|
0.7
|
CX
|
A:ICH503
|
1.9
|
8.4
|
0.3
|
S4A
|
A:ICS502
|
2.2
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
2.2
|
9.4
|
0.3
|
S5A
|
A:ICS502
|
2.2
|
7.8
|
0.6
|
S2A
|
A:ICS502
|
2.3
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.3
|
8.7
|
0.3
|
SE5A
|
A:ICH503
|
2.3
|
10.5
|
0.4
|
FE7
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
FE2
|
A:ICS502
|
2.6
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
2.6
|
8.5
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE1
|
A:ICS502
|
2.7
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
2.7
|
9.1
|
0.3
|
FE6
|
A:ICS502
|
3.7
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
3.7
|
8.9
|
0.3
|
FE5
|
A:ICS502
|
3.7
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
3.7
|
8.7
|
0.3
|
S1A
|
A:ICS502
|
3.9
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
3.9
|
8.7
|
0.3
|
O
|
A:HOH921
|
4.1
|
9.4
|
1.0
|
NH2
|
A:ARG96
|
4.1
|
9.6
|
1.0
|
CD2
|
A:TYR229
|
4.1
|
9.3
|
1.0
|
C
|
A:CMO506
|
4.1
|
7.6
|
0.9
|
S3B
|
A:ICS502
|
4.2
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
4.2
|
8.4
|
0.3
|
S4B
|
A:ICS502
|
4.3
|
8.5
|
0.7
|
S4B
|
A:ICH503
|
4.3
|
8.5
|
0.3
|
CE2
|
A:TYR229
|
4.5
|
9.2
|
1.0
|
S3A
|
A:ICS502
|
4.5
|
7.6
|
0.7
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
SE2B
|
A:ICH503
|
4.6
|
4.2
|
0.1
|
SG
|
A:CYS275
|
4.8
|
8.4
|
1.0
|
|
Iron binding site 10 out
of 46 in 5bvh
Go back to
Iron Binding Sites List in 5bvh
Iron binding site 10 out
of 46 in the Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 10 of Co-Bound Form of Selenium Incorporated Nitrogenase Mofe-Protein (AV1- Se-Co) From A. Vinelandii within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe503
b:8.5
occ:0.35
|
FE2
|
A:ICS502
|
0.0
|
8.5
|
0.7
|
FE2
|
A:ICH503
|
0.0
|
8.5
|
0.3
|
C
|
A:CMO506
|
1.9
|
7.6
|
0.9
|
CX
|
A:ICS502
|
2.0
|
8.4
|
0.7
|
CX
|
A:ICH503
|
2.0
|
8.4
|
0.3
|
S2A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S2A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
S1A
|
A:ICS502
|
2.2
|
8.7
|
0.7
|
S1A
|
A:ICH503
|
2.2
|
8.7
|
0.3
|
SE2B
|
A:ICH503
|
2.3
|
4.2
|
0.1
|
FE6
|
A:ICS502
|
2.5
|
8.9
|
0.7
|
FE6
|
A:ICH503
|
2.5
|
8.9
|
0.3
|
FE1
|
A:ICS502
|
2.6
|
9.1
|
0.7
|
FE1
|
A:ICH503
|
2.6
|
9.1
|
0.3
|
FE4
|
A:ICS502
|
2.6
|
8.7
|
0.7
|
FE4
|
A:ICH503
|
2.6
|
8.7
|
0.3
|
FE3
|
A:ICS502
|
2.6
|
8.6
|
0.7
|
FE3
|
A:ICH503
|
2.6
|
8.6
|
0.3
|
O
|
A:CMO506
|
2.9
|
8.2
|
0.9
|
FE7
|
A:ICS502
|
3.6
|
8.6
|
0.7
|
FE7
|
A:ICH503
|
3.6
|
8.6
|
0.3
|
FE5
|
A:ICS502
|
3.6
|
8.7
|
0.7
|
FE5
|
A:ICH503
|
3.6
|
8.7
|
0.3
|
S4A
|
A:ICS502
|
3.8
|
9.4
|
0.7
|
S4A
|
A:ICH503
|
3.8
|
9.4
|
0.3
|
CZ
|
A:PHE381
|
4.0
|
8.6
|
1.0
|
S1B
|
A:ICS502
|
4.1
|
8.3
|
0.7
|
S1B
|
A:ICH503
|
4.1
|
8.3
|
0.3
|
S3B
|
A:ICS502
|
4.1
|
8.4
|
0.7
|
S3B
|
A:ICH503
|
4.1
|
8.4
|
0.3
|
NE2
|
A:HIS195
|
4.2
|
10.8
|
1.0
|
CE1
|
A:HIS195
|
4.4
|
10.8
|
1.0
|
CG1
|
A:VAL70
|
4.4
|
10.4
|
1.0
|
S5A
|
A:ICS502
|
4.5
|
7.8
|
0.6
|
S3A
|
A:ICS502
|
4.5
|
7.6
|
0.7
|
CE1
|
A:PHE381
|
4.5
|
8.6
|
1.0
|
SE3A
|
A:ICH503
|
4.6
|
9.5
|
0.3
|
SE5A
|
A:ICH503
|
4.6
|
10.5
|
0.4
|
SG
|
A:CYS275
|
4.6
|
8.4
|
1.0
|
MO1
|
A:ICS502
|
4.9
|
8.1
|
0.7
|
MO1
|
A:ICH503
|
4.9
|
8.1
|
0.3
|
CG2
|
A:VAL70
|
5.0
|
10.4
|
1.0
|
N
|
A:GLY357
|
5.0
|
8.6
|
1.0
|
|
Reference:
T.Spatzal,
K.A.Perez,
J.B.Howard,
D.C.Rees.
Catalysis-Dependent Selenium Incorporation and Migration in the Nitrogenase Active Site Iron-Molybdenum Cofactor. Elife V. 4 11620 2015.
ISSN: ESSN 2050-084X
PubMed: 26673079
DOI: 10.7554/ELIFE.11620
Page generated: Mon Aug 5 20:09:08 2024
|