Iron in PDB 1e39: Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
Enzymatic activity of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
All present enzymatic activity of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine:
1.3.99.1;
Protein crystallography data
The structure of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine, PDB code: 1e39
was solved by
M.K.Doherty,
S.L.Pealing,
C.S.Miles,
R.Moysey,
P.Taylor,
M.D.Walkinshaw,
G.A.Reid,
S.K.Chapman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
18.00 /
1.80
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
45.571,
92.172,
78.489,
90.00,
91.08,
90.00
|
R / Rfree (%)
|
18.1 /
24.7
|
Other elements in 1e39:
The structure of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
(pdb code 1e39). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine, PDB code: 1e39:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1e39
Go back to
Iron Binding Sites List in 1e39
Iron binding site 1 out
of 4 in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe801
b:15.7
occ:1.00
|
FE
|
A:HEC801
|
0.0
|
15.7
|
1.0
|
NA
|
A:HEC801
|
1.9
|
14.1
|
1.0
|
NC
|
A:HEC801
|
1.9
|
17.6
|
1.0
|
NE2
|
A:HIS18
|
1.9
|
16.0
|
1.0
|
NE2
|
A:HIS75
|
2.0
|
18.5
|
1.0
|
ND
|
A:HEC801
|
2.0
|
11.9
|
1.0
|
NB
|
A:HEC801
|
2.0
|
17.3
|
1.0
|
CE1
|
A:HIS18
|
2.8
|
19.3
|
1.0
|
CE1
|
A:HIS75
|
2.9
|
17.1
|
1.0
|
C1A
|
A:HEC801
|
3.0
|
18.7
|
1.0
|
C4A
|
A:HEC801
|
3.0
|
23.1
|
1.0
|
C4C
|
A:HEC801
|
3.0
|
20.9
|
1.0
|
C1C
|
A:HEC801
|
3.0
|
21.8
|
1.0
|
C1D
|
A:HEC801
|
3.0
|
14.1
|
1.0
|
C1B
|
A:HEC801
|
3.1
|
19.3
|
1.0
|
C4D
|
A:HEC801
|
3.1
|
12.4
|
1.0
|
CD2
|
A:HIS75
|
3.1
|
12.0
|
1.0
|
C4B
|
A:HEC801
|
3.1
|
19.8
|
1.0
|
CD2
|
A:HIS18
|
3.1
|
15.4
|
1.0
|
CHD
|
A:HEC801
|
3.4
|
16.5
|
1.0
|
CHA
|
A:HEC801
|
3.4
|
17.6
|
1.0
|
CHC
|
A:HEC801
|
3.4
|
18.3
|
1.0
|
CHB
|
A:HEC801
|
3.4
|
17.7
|
1.0
|
ND1
|
A:HIS18
|
4.0
|
20.8
|
1.0
|
ND1
|
A:HIS75
|
4.1
|
16.7
|
1.0
|
CG
|
A:HIS75
|
4.2
|
16.4
|
1.0
|
CG
|
A:HIS18
|
4.2
|
15.1
|
1.0
|
C2A
|
A:HEC801
|
4.2
|
18.4
|
1.0
|
C3A
|
A:HEC801
|
4.2
|
21.7
|
1.0
|
C2C
|
A:HEC801
|
4.2
|
14.2
|
1.0
|
C3C
|
A:HEC801
|
4.2
|
19.2
|
1.0
|
C2D
|
A:HEC801
|
4.3
|
15.9
|
1.0
|
C3D
|
A:HEC801
|
4.3
|
11.2
|
1.0
|
C2B
|
A:HEC801
|
4.3
|
19.9
|
1.0
|
C3B
|
A:HEC801
|
4.3
|
16.4
|
1.0
|
O
|
A:HOH2036
|
4.9
|
28.8
|
1.0
|
|
Iron binding site 2 out
of 4 in 1e39
Go back to
Iron Binding Sites List in 1e39
Iron binding site 2 out
of 4 in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe802
b:19.0
occ:1.00
|
FE
|
A:HEC802
|
0.0
|
19.0
|
1.0
|
NC
|
A:HEC802
|
1.9
|
16.6
|
1.0
|
NA
|
A:HEC802
|
1.9
|
13.1
|
1.0
|
ND
|
A:HEC802
|
2.0
|
19.1
|
1.0
|
NE2
|
A:HIS40
|
2.0
|
22.7
|
1.0
|
NB
|
A:HEC802
|
2.1
|
11.2
|
1.0
|
NE2
|
A:HIS8
|
2.1
|
13.7
|
1.0
|
C4C
|
A:HEC802
|
2.9
|
30.1
|
1.0
|
C1A
|
A:HEC802
|
2.9
|
24.1
|
1.0
|
C4A
|
A:HEC802
|
3.0
|
19.1
|
1.0
|
C1C
|
A:HEC802
|
3.0
|
22.5
|
1.0
|
CE1
|
A:HIS40
|
3.0
|
14.3
|
1.0
|
C1D
|
A:HEC802
|
3.0
|
17.4
|
1.0
|
C4D
|
A:HEC802
|
3.0
|
17.7
|
1.0
|
CD2
|
A:HIS40
|
3.0
|
12.7
|
1.0
|
C4B
|
A:HEC802
|
3.1
|
14.3
|
1.0
|
CD2
|
A:HIS8
|
3.1
|
19.6
|
1.0
|
CE1
|
A:HIS8
|
3.1
|
14.1
|
1.0
|
C1B
|
A:HEC802
|
3.1
|
12.8
|
1.0
|
CHD
|
A:HEC802
|
3.3
|
21.2
|
1.0
|
CHA
|
A:HEC802
|
3.4
|
17.6
|
1.0
|
CHC
|
A:HEC802
|
3.4
|
19.8
|
1.0
|
CHB
|
A:HEC802
|
3.4
|
12.9
|
1.0
|
ND1
|
A:HIS40
|
4.1
|
16.6
|
1.0
|
C3C
|
A:HEC802
|
4.1
|
27.1
|
1.0
|
CG
|
A:HIS40
|
4.2
|
15.7
|
1.0
|
C2C
|
A:HEC802
|
4.2
|
22.1
|
1.0
|
C3A
|
A:HEC802
|
4.2
|
22.1
|
1.0
|
C2A
|
A:HEC802
|
4.2
|
23.2
|
1.0
|
ND1
|
A:HIS8
|
4.2
|
18.4
|
1.0
|
C2D
|
A:HEC802
|
4.2
|
24.7
|
1.0
|
CG
|
A:HIS8
|
4.2
|
17.5
|
1.0
|
C3D
|
A:HEC802
|
4.2
|
23.8
|
1.0
|
C3B
|
A:HEC802
|
4.3
|
13.0
|
1.0
|
C2B
|
A:HEC802
|
4.3
|
12.5
|
1.0
|
|
Iron binding site 3 out
of 4 in 1e39
Go back to
Iron Binding Sites List in 1e39
Iron binding site 3 out
of 4 in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe803
b:16.1
occ:1.00
|
FE
|
A:HEC803
|
0.0
|
16.1
|
1.0
|
ND
|
A:HEC803
|
1.9
|
12.9
|
1.0
|
NB
|
A:HEC803
|
1.9
|
13.2
|
1.0
|
NA
|
A:HEC803
|
2.0
|
16.0
|
1.0
|
NC
|
A:HEC803
|
2.1
|
11.9
|
1.0
|
NE2
|
A:HIS58
|
2.1
|
22.6
|
1.0
|
NE2
|
A:HIS72
|
2.1
|
14.7
|
1.0
|
C4D
|
A:HEC803
|
2.9
|
22.5
|
1.0
|
CE1
|
A:HIS58
|
2.9
|
22.9
|
1.0
|
C1B
|
A:HEC803
|
2.9
|
20.8
|
1.0
|
C1D
|
A:HEC803
|
3.0
|
26.0
|
1.0
|
C4B
|
A:HEC803
|
3.0
|
13.4
|
1.0
|
CE1
|
A:HIS72
|
3.0
|
18.3
|
1.0
|
C1A
|
A:HEC803
|
3.1
|
24.9
|
1.0
|
C1C
|
A:HEC803
|
3.1
|
10.3
|
1.0
|
C4A
|
A:HEC803
|
3.1
|
17.6
|
1.0
|
C4C
|
A:HEC803
|
3.1
|
14.8
|
1.0
|
CD2
|
A:HIS72
|
3.1
|
13.9
|
1.0
|
CD2
|
A:HIS58
|
3.2
|
20.6
|
1.0
|
CHA
|
A:HEC803
|
3.4
|
25.4
|
1.0
|
CHB
|
A:HEC803
|
3.4
|
20.1
|
1.0
|
CHC
|
A:HEC803
|
3.4
|
10.1
|
1.0
|
CHD
|
A:HEC803
|
3.4
|
15.2
|
1.0
|
ND1
|
A:HIS58
|
4.1
|
14.7
|
1.0
|
ND1
|
A:HIS72
|
4.2
|
16.8
|
1.0
|
C3D
|
A:HEC803
|
4.2
|
21.2
|
1.0
|
C2D
|
A:HEC803
|
4.2
|
19.2
|
1.0
|
C2B
|
A:HEC803
|
4.2
|
15.9
|
1.0
|
C3B
|
A:HEC803
|
4.2
|
14.1
|
1.0
|
CG
|
A:HIS72
|
4.2
|
14.0
|
1.0
|
CG
|
A:HIS58
|
4.3
|
10.4
|
1.0
|
C3A
|
A:HEC803
|
4.3
|
18.6
|
1.0
|
C2A
|
A:HEC803
|
4.3
|
17.7
|
1.0
|
C2C
|
A:HEC803
|
4.3
|
12.4
|
1.0
|
C3C
|
A:HEC803
|
4.3
|
9.2
|
1.0
|
|
Iron binding site 4 out
of 4 in 1e39
Go back to
Iron Binding Sites List in 1e39
Iron binding site 4 out
of 4 in the Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Flavocytochrome C3 From Shewanella Frigidimarina Histidine 365 Mutated to Alanine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe804
b:11.5
occ:1.00
|
FE
|
A:HEC804
|
0.0
|
11.5
|
1.0
|
NE2
|
A:HIS61
|
1.9
|
11.1
|
1.0
|
ND
|
A:HEC804
|
1.9
|
13.3
|
1.0
|
NE2
|
A:HIS86
|
1.9
|
13.6
|
1.0
|
NA
|
A:HEC804
|
1.9
|
16.1
|
1.0
|
NC
|
A:HEC804
|
2.0
|
11.2
|
1.0
|
NB
|
A:HEC804
|
2.0
|
11.4
|
1.0
|
CE1
|
A:HIS61
|
2.9
|
10.3
|
1.0
|
CE1
|
A:HIS86
|
2.9
|
13.7
|
1.0
|
C4D
|
A:HEC804
|
2.9
|
14.3
|
1.0
|
CD2
|
A:HIS61
|
2.9
|
11.7
|
1.0
|
C1D
|
A:HEC804
|
3.0
|
12.0
|
1.0
|
C1A
|
A:HEC804
|
3.0
|
19.4
|
1.0
|
CD2
|
A:HIS86
|
3.0
|
10.8
|
1.0
|
C4A
|
A:HEC804
|
3.0
|
16.1
|
1.0
|
C4C
|
A:HEC804
|
3.0
|
12.1
|
1.0
|
C1C
|
A:HEC804
|
3.1
|
10.0
|
1.0
|
C1B
|
A:HEC804
|
3.1
|
18.0
|
1.0
|
C4B
|
A:HEC804
|
3.1
|
13.5
|
1.0
|
CHA
|
A:HEC804
|
3.3
|
18.5
|
1.0
|
CHD
|
A:HEC804
|
3.4
|
14.3
|
1.0
|
CHB
|
A:HEC804
|
3.4
|
15.1
|
1.0
|
CHC
|
A:HEC804
|
3.4
|
17.1
|
1.0
|
ND1
|
A:HIS61
|
4.0
|
13.2
|
1.0
|
ND1
|
A:HIS86
|
4.0
|
16.9
|
1.0
|
CG
|
A:HIS61
|
4.1
|
14.0
|
1.0
|
CG
|
A:HIS86
|
4.1
|
17.4
|
1.0
|
C3D
|
A:HEC804
|
4.2
|
9.8
|
1.0
|
C2D
|
A:HEC804
|
4.2
|
11.8
|
1.0
|
C2A
|
A:HEC804
|
4.2
|
12.9
|
1.0
|
C3A
|
A:HEC804
|
4.2
|
15.6
|
1.0
|
C3C
|
A:HEC804
|
4.3
|
11.2
|
1.0
|
C2C
|
A:HEC804
|
4.3
|
12.8
|
1.0
|
C2B
|
A:HEC804
|
4.3
|
15.6
|
1.0
|
C3B
|
A:HEC804
|
4.3
|
10.1
|
1.0
|
|
Reference:
M.K.Doherty,
S.L.Pealing,
C.S.Miles,
R.Moysey,
P.Taylor,
M.D.Walkinshaw,
G.A.Reid,
S.K.Chapman.
Identification of the Active Site Acid/Base Catalyst in A Bacterial Fumarate Reductase: A Kinetic and Crystallographic Study Biochemistry V. 39 10695 2000.
ISSN: ISSN 0006-2960
PubMed: 10978153
DOI: 10.1021/BI000871L
Page generated: Sat Aug 3 04:11:50 2024
|