Iron in PDB 3sxt: Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
Enzymatic activity of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
All present enzymatic activity of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug:
1.4.99.3;
Protein crystallography data
The structure of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug, PDB code: 3sxt
was solved by
L.M.R.Jensen,
C.M.Wilmot,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
35.01 /
1.81
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
62.639,
135.664,
111.557,
90.00,
97.37,
90.00
|
R / Rfree (%)
|
14.5 /
18.7
|
Other elements in 3sxt:
The structure of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
(pdb code 3sxt). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug, PDB code: 3sxt:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 3sxt
Go back to
Iron Binding Sites List in 3sxt
Iron binding site 1 out
of 4 in the Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe404
b:28.6
occ:1.00
|
FE
|
A:HEC404
|
0.0
|
28.6
|
1.0
|
NC
|
A:HEC404
|
2.1
|
30.9
|
1.0
|
ND
|
A:HEC404
|
2.1
|
28.7
|
1.0
|
NA
|
A:HEC404
|
2.1
|
31.4
|
1.0
|
NB
|
A:HEC404
|
2.1
|
28.2
|
1.0
|
O
|
A:HOH834
|
2.1
|
36.9
|
1.0
|
NE2
|
A:HIS35
|
2.1
|
28.8
|
1.0
|
C4B
|
A:HEC404
|
3.0
|
28.8
|
1.0
|
C4D
|
A:HEC404
|
3.1
|
30.6
|
1.0
|
CD2
|
A:HIS35
|
3.1
|
26.6
|
1.0
|
C4C
|
A:HEC404
|
3.1
|
31.8
|
1.0
|
C1A
|
A:HEC404
|
3.1
|
29.3
|
1.0
|
C1B
|
A:HEC404
|
3.1
|
29.2
|
1.0
|
C4A
|
A:HEC404
|
3.1
|
32.5
|
1.0
|
C1C
|
A:HEC404
|
3.1
|
30.7
|
1.0
|
C1D
|
A:HEC404
|
3.1
|
30.0
|
1.0
|
CE1
|
A:HIS35
|
3.1
|
28.0
|
1.0
|
CHC
|
A:HEC404
|
3.4
|
28.7
|
1.0
|
CHD
|
A:HEC404
|
3.4
|
30.0
|
1.0
|
CHA
|
A:HEC404
|
3.4
|
26.4
|
1.0
|
CHB
|
A:HEC404
|
3.5
|
28.0
|
1.0
|
O
|
A:HOH562
|
4.0
|
31.5
|
1.0
|
NE2
|
A:GLN103
|
4.1
|
33.4
|
1.0
|
ND1
|
A:HIS35
|
4.2
|
27.4
|
1.0
|
CG
|
A:HIS35
|
4.2
|
28.5
|
1.0
|
C3C
|
A:HEC404
|
4.3
|
28.0
|
1.0
|
C3D
|
A:HEC404
|
4.3
|
28.4
|
1.0
|
C2B
|
A:HEC404
|
4.4
|
29.8
|
1.0
|
C2D
|
A:HEC404
|
4.4
|
29.3
|
1.0
|
C3B
|
A:HEC404
|
4.4
|
28.6
|
1.0
|
C2A
|
A:HEC404
|
4.4
|
28.8
|
1.0
|
C3A
|
A:HEC404
|
4.4
|
28.0
|
1.0
|
C2C
|
A:HEC404
|
4.4
|
32.2
|
1.0
|
CG
|
A:PRO107
|
4.4
|
33.5
|
1.0
|
CB
|
A:PRO107
|
5.0
|
35.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 3sxt
Go back to
Iron Binding Sites List in 3sxt
Iron binding site 2 out
of 4 in the Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe405
b:23.4
occ:1.00
|
FE
|
A:HEC405
|
0.0
|
23.4
|
1.0
|
OH
|
A:TYR294
|
2.0
|
21.7
|
1.0
|
NC
|
A:HEC405
|
2.0
|
21.7
|
1.0
|
ND
|
A:HEC405
|
2.0
|
24.0
|
1.0
|
NE2
|
A:HIS205
|
2.1
|
23.9
|
1.0
|
NA
|
A:HEC405
|
2.1
|
24.7
|
1.0
|
NB
|
A:HEC405
|
2.1
|
22.1
|
1.0
|
CZ
|
A:TYR294
|
2.9
|
22.2
|
1.0
|
CD2
|
A:HIS205
|
3.0
|
24.0
|
1.0
|
C4C
|
A:HEC405
|
3.0
|
22.1
|
1.0
|
C1D
|
A:HEC405
|
3.1
|
22.4
|
1.0
|
C4A
|
A:HEC405
|
3.1
|
24.5
|
1.0
|
C1A
|
A:HEC405
|
3.1
|
22.3
|
1.0
|
C4D
|
A:HEC405
|
3.1
|
22.3
|
1.0
|
C1B
|
A:HEC405
|
3.1
|
20.1
|
1.0
|
C1C
|
A:HEC405
|
3.1
|
21.6
|
1.0
|
CE1
|
A:HIS205
|
3.1
|
24.9
|
1.0
|
C4B
|
A:HEC405
|
3.1
|
22.0
|
1.0
|
CHD
|
A:HEC405
|
3.4
|
20.7
|
1.0
|
CHA
|
A:HEC405
|
3.4
|
20.7
|
1.0
|
CHB
|
A:HEC405
|
3.4
|
22.8
|
1.0
|
CHC
|
A:HEC405
|
3.5
|
21.9
|
1.0
|
CE1
|
A:TYR294
|
3.6
|
21.9
|
1.0
|
CE2
|
A:TYR294
|
3.7
|
22.0
|
1.0
|
CG
|
A:HIS205
|
4.1
|
23.9
|
1.0
|
ND1
|
A:HIS205
|
4.2
|
23.9
|
1.0
|
C2A
|
A:HEC405
|
4.3
|
21.2
|
1.0
|
C3A
|
A:HEC405
|
4.3
|
23.4
|
1.0
|
C3C
|
A:HEC405
|
4.3
|
24.0
|
1.0
|
C2D
|
A:HEC405
|
4.3
|
23.8
|
1.0
|
C3D
|
A:HEC405
|
4.3
|
22.3
|
1.0
|
C2B
|
A:HEC405
|
4.4
|
22.4
|
1.0
|
C2C
|
A:HEC405
|
4.4
|
25.2
|
1.0
|
C3B
|
A:HEC405
|
4.4
|
22.4
|
1.0
|
CD1
|
A:TYR294
|
4.8
|
22.2
|
1.0
|
CD1
|
A:ILE226
|
5.0
|
24.2
|
1.0
|
CD2
|
A:TYR294
|
5.0
|
22.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 3sxt
Go back to
Iron Binding Sites List in 3sxt
Iron binding site 3 out
of 4 in the Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe404
b:27.9
occ:1.00
|
FE
|
B:HEC404
|
0.0
|
27.9
|
1.0
|
NB
|
B:HEC404
|
2.0
|
25.2
|
1.0
|
ND
|
B:HEC404
|
2.1
|
27.4
|
1.0
|
NA
|
B:HEC404
|
2.1
|
29.3
|
1.0
|
NC
|
B:HEC404
|
2.1
|
28.7
|
1.0
|
NE2
|
B:HIS35
|
2.1
|
30.5
|
1.0
|
C4C
|
B:HEC404
|
3.0
|
29.4
|
1.0
|
C4B
|
B:HEC404
|
3.1
|
27.9
|
1.0
|
C4D
|
B:HEC404
|
3.1
|
29.9
|
1.0
|
C1A
|
B:HEC404
|
3.1
|
28.9
|
1.0
|
C4A
|
B:HEC404
|
3.1
|
25.6
|
1.0
|
C1C
|
B:HEC404
|
3.1
|
28.1
|
1.0
|
C1B
|
B:HEC404
|
3.1
|
25.1
|
1.0
|
CE1
|
B:HIS35
|
3.1
|
26.2
|
1.0
|
C1D
|
B:HEC404
|
3.1
|
28.3
|
1.0
|
CD2
|
B:HIS35
|
3.1
|
27.7
|
1.0
|
CHD
|
B:HEC404
|
3.4
|
29.4
|
1.0
|
CHA
|
B:HEC404
|
3.4
|
26.6
|
1.0
|
CHC
|
B:HEC404
|
3.5
|
30.2
|
1.0
|
CHB
|
B:HEC404
|
3.5
|
22.6
|
1.0
|
O
|
B:HOH815
|
3.9
|
30.9
|
1.0
|
NE2
|
B:GLN103
|
4.1
|
26.3
|
1.0
|
ND1
|
B:HIS35
|
4.2
|
30.1
|
1.0
|
CG
|
B:HIS35
|
4.2
|
30.1
|
1.0
|
CG
|
B:PRO107
|
4.3
|
32.5
|
1.0
|
C3C
|
B:HEC404
|
4.3
|
27.1
|
1.0
|
C2C
|
B:HEC404
|
4.3
|
29.9
|
1.0
|
C3B
|
B:HEC404
|
4.3
|
29.0
|
1.0
|
C2A
|
B:HEC404
|
4.4
|
25.0
|
1.0
|
C3D
|
B:HEC404
|
4.4
|
27.7
|
1.0
|
C3A
|
B:HEC404
|
4.4
|
24.2
|
1.0
|
C2B
|
B:HEC404
|
4.4
|
24.4
|
1.0
|
C2D
|
B:HEC404
|
4.4
|
28.4
|
1.0
|
CB
|
B:PRO107
|
4.8
|
34.0
|
1.0
|
|
Iron binding site 4 out
of 4 in 3sxt
Go back to
Iron Binding Sites List in 3sxt
Iron binding site 4 out
of 4 in the Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe405
b:21.5
occ:1.00
|
FE
|
B:HEC405
|
0.0
|
21.5
|
1.0
|
OH
|
B:TYR294
|
2.0
|
22.6
|
1.0
|
NB
|
B:HEC405
|
2.0
|
21.4
|
1.0
|
NC
|
B:HEC405
|
2.0
|
22.6
|
1.0
|
ND
|
B:HEC405
|
2.0
|
21.5
|
1.0
|
NA
|
B:HEC405
|
2.0
|
19.8
|
1.0
|
NE2
|
B:HIS205
|
2.1
|
18.6
|
1.0
|
CZ
|
B:TYR294
|
2.9
|
17.4
|
1.0
|
C4A
|
B:HEC405
|
3.0
|
20.4
|
1.0
|
C4C
|
B:HEC405
|
3.0
|
19.7
|
1.0
|
CD2
|
B:HIS205
|
3.0
|
20.4
|
1.0
|
C1C
|
B:HEC405
|
3.0
|
21.8
|
1.0
|
C1B
|
B:HEC405
|
3.1
|
22.7
|
1.0
|
C1A
|
B:HEC405
|
3.1
|
18.4
|
1.0
|
C4D
|
B:HEC405
|
3.1
|
22.3
|
1.0
|
C1D
|
B:HEC405
|
3.1
|
21.7
|
1.0
|
C4B
|
B:HEC405
|
3.1
|
17.9
|
1.0
|
CE1
|
B:HIS205
|
3.1
|
19.4
|
1.0
|
CHD
|
B:HEC405
|
3.4
|
19.8
|
1.0
|
CHB
|
B:HEC405
|
3.4
|
18.5
|
1.0
|
CHA
|
B:HEC405
|
3.4
|
20.2
|
1.0
|
CHC
|
B:HEC405
|
3.5
|
19.0
|
1.0
|
CE1
|
B:TYR294
|
3.6
|
21.9
|
1.0
|
CE2
|
B:TYR294
|
3.8
|
17.8
|
1.0
|
CG
|
B:HIS205
|
4.2
|
22.3
|
1.0
|
ND1
|
B:HIS205
|
4.2
|
18.9
|
1.0
|
C3A
|
B:HEC405
|
4.3
|
18.6
|
1.0
|
C3C
|
B:HEC405
|
4.3
|
19.4
|
1.0
|
C2A
|
B:HEC405
|
4.3
|
21.0
|
1.0
|
C2B
|
B:HEC405
|
4.3
|
20.3
|
1.0
|
C3D
|
B:HEC405
|
4.3
|
21.1
|
1.0
|
C2C
|
B:HEC405
|
4.3
|
19.5
|
1.0
|
C3B
|
B:HEC405
|
4.4
|
19.3
|
1.0
|
C2D
|
B:HEC405
|
4.4
|
23.9
|
1.0
|
CD1
|
B:TYR294
|
4.8
|
19.4
|
1.0
|
|
Reference:
L.M.R.Jensen,
C.M.Wilmot.
Crystal Structure of the Quinol Form of Methylamine Dehydrogenase in Complex with the Diferrous Form of Maug To Be Published.
Page generated: Sun Aug 4 20:06:04 2024
|