Iron in PDB 4o1q: Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
Enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
All present enzymatic activity of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;
Protein crystallography data
The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q
was solved by
E.T.Yukl,
C.W.Wilmot,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
44.49 /
2.59
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.530,
83.520,
107.780,
109.94,
91.54,
105.78
|
R / Rfree (%)
|
19.8 /
25.4
|
Other elements in 4o1q:
The structure of Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
(pdb code 4o1q). 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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 4o1q:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 4o1q
Go back to
Iron Binding Sites List in 4o1q
Iron binding site 1 out
of 4 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe402
b:49.0
occ:1.00
|
FE
|
A:HEC402
|
0.0
|
49.0
|
1.0
|
ND
|
A:HEC402
|
2.1
|
48.9
|
1.0
|
NC
|
A:HEC402
|
2.1
|
50.6
|
1.0
|
NB
|
A:HEC402
|
2.1
|
49.4
|
1.0
|
NA
|
A:HEC402
|
2.1
|
47.9
|
1.0
|
NE2
|
A:HIS35
|
2.3
|
49.1
|
1.0
|
C4D
|
A:HEC402
|
3.1
|
48.3
|
1.0
|
C1C
|
A:HEC402
|
3.1
|
51.3
|
1.0
|
C4B
|
A:HEC402
|
3.1
|
50.2
|
1.0
|
C4A
|
A:HEC402
|
3.1
|
47.7
|
1.0
|
CD2
|
A:HIS35
|
3.1
|
49.9
|
1.0
|
C1D
|
A:HEC402
|
3.1
|
49.8
|
1.0
|
C1A
|
A:HEC402
|
3.1
|
47.3
|
1.0
|
C4C
|
A:HEC402
|
3.1
|
51.2
|
1.0
|
C1B
|
A:HEC402
|
3.1
|
49.0
|
1.0
|
O
|
A:HOH563
|
3.4
|
40.4
|
1.0
|
CE1
|
A:HIS35
|
3.4
|
48.8
|
1.0
|
CHC
|
A:HEC402
|
3.4
|
51.1
|
1.0
|
CHA
|
A:HEC402
|
3.4
|
47.5
|
1.0
|
CHB
|
A:HEC402
|
3.5
|
48.2
|
1.0
|
CHD
|
A:HEC402
|
3.5
|
50.8
|
1.0
|
O
|
A:HOH535
|
3.5
|
48.3
|
1.0
|
CG
|
A:PRO107
|
4.0
|
53.5
|
1.0
|
CG
|
A:HIS35
|
4.3
|
50.0
|
1.0
|
C3D
|
A:HEC402
|
4.4
|
48.5
|
1.0
|
C2C
|
A:HEC402
|
4.4
|
52.4
|
1.0
|
C2D
|
A:HEC402
|
4.4
|
49.6
|
1.0
|
C3A
|
A:HEC402
|
4.4
|
47.0
|
1.0
|
C2A
|
A:HEC402
|
4.4
|
46.7
|
1.0
|
C3C
|
A:HEC402
|
4.4
|
52.4
|
1.0
|
ND1
|
A:HIS35
|
4.4
|
49.3
|
1.0
|
C3B
|
A:HEC402
|
4.4
|
50.4
|
1.0
|
C2B
|
A:HEC402
|
4.4
|
49.7
|
1.0
|
CB
|
A:PRO107
|
4.7
|
54.5
|
1.0
|
CG2
|
A:THR67
|
4.8
|
51.0
|
1.0
|
|
Iron binding site 2 out
of 4 in 4o1q
Go back to
Iron Binding Sites List in 4o1q
Iron binding site 2 out
of 4 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe403
b:44.8
occ:1.00
|
FE
|
A:HEC403
|
0.0
|
44.8
|
1.0
|
OH
|
A:TYR294
|
1.9
|
45.6
|
1.0
|
NB
|
A:HEC403
|
2.1
|
45.4
|
1.0
|
NA
|
A:HEC403
|
2.1
|
45.3
|
1.0
|
ND
|
A:HEC403
|
2.1
|
44.4
|
1.0
|
NC
|
A:HEC403
|
2.1
|
44.6
|
1.0
|
NE2
|
A:HIS205
|
2.4
|
45.1
|
1.0
|
CZ
|
A:TYR294
|
2.8
|
46.2
|
1.0
|
C4B
|
A:HEC403
|
3.1
|
45.6
|
1.0
|
C1A
|
A:HEC403
|
3.1
|
45.4
|
1.0
|
C1B
|
A:HEC403
|
3.1
|
46.0
|
1.0
|
C4D
|
A:HEC403
|
3.1
|
44.6
|
1.0
|
C4C
|
A:HEC403
|
3.1
|
44.4
|
1.0
|
C4A
|
A:HEC403
|
3.1
|
45.9
|
1.0
|
C1C
|
A:HEC403
|
3.1
|
44.9
|
1.0
|
C1D
|
A:HEC403
|
3.1
|
44.1
|
1.0
|
CD2
|
A:HIS205
|
3.1
|
45.2
|
1.0
|
CHA
|
A:HEC403
|
3.4
|
45.1
|
1.0
|
CHC
|
A:HEC403
|
3.5
|
45.4
|
1.0
|
CHB
|
A:HEC403
|
3.5
|
46.1
|
1.0
|
CHD
|
A:HEC403
|
3.5
|
44.1
|
1.0
|
CE2
|
A:TYR294
|
3.5
|
46.9
|
1.0
|
CE1
|
A:HIS205
|
3.5
|
44.9
|
1.0
|
CE1
|
A:TYR294
|
3.7
|
46.2
|
1.0
|
CG
|
A:HIS205
|
4.4
|
45.1
|
1.0
|
C3B
|
A:HEC403
|
4.4
|
46.4
|
1.0
|
C3C
|
A:HEC403
|
4.4
|
44.6
|
1.0
|
C2B
|
A:HEC403
|
4.4
|
46.6
|
1.0
|
C2A
|
A:HEC403
|
4.4
|
46.0
|
1.0
|
C3A
|
A:HEC403
|
4.4
|
46.3
|
1.0
|
C3D
|
A:HEC403
|
4.4
|
44.4
|
1.0
|
C2D
|
A:HEC403
|
4.4
|
44.1
|
1.0
|
C2C
|
A:HEC403
|
4.4
|
44.8
|
1.0
|
ND1
|
A:HIS205
|
4.5
|
44.9
|
1.0
|
CD2
|
A:TYR294
|
4.7
|
47.6
|
1.0
|
CD1
|
A:TYR294
|
4.8
|
46.9
|
1.0
|
CD1
|
A:ILE226
|
5.0
|
46.1
|
1.0
|
|
Iron binding site 3 out
of 4 in 4o1q
Go back to
Iron Binding Sites List in 4o1q
Iron binding site 3 out
of 4 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe402
b:41.3
occ:1.00
|
FE
|
B:HEC402
|
0.0
|
41.3
|
1.0
|
NC
|
B:HEC402
|
2.1
|
42.7
|
1.0
|
ND
|
B:HEC402
|
2.1
|
41.4
|
1.0
|
NA
|
B:HEC402
|
2.1
|
40.7
|
1.0
|
NB
|
B:HEC402
|
2.1
|
41.6
|
1.0
|
NE2
|
B:HIS35
|
2.2
|
40.6
|
1.0
|
CD2
|
B:HIS35
|
3.0
|
41.2
|
1.0
|
C4D
|
B:HEC402
|
3.1
|
41.0
|
1.0
|
C1C
|
B:HEC402
|
3.1
|
43.4
|
1.0
|
C4C
|
B:HEC402
|
3.1
|
43.3
|
1.0
|
C4A
|
B:HEC402
|
3.1
|
40.6
|
1.0
|
C4B
|
B:HEC402
|
3.1
|
42.3
|
1.0
|
C1A
|
B:HEC402
|
3.1
|
40.3
|
1.0
|
C1D
|
B:HEC402
|
3.1
|
42.0
|
1.0
|
C1B
|
B:HEC402
|
3.1
|
41.4
|
1.0
|
O
|
B:HOH573
|
3.1
|
47.8
|
1.0
|
CE1
|
B:HIS35
|
3.3
|
40.1
|
1.0
|
CHD
|
B:HEC402
|
3.4
|
43.0
|
1.0
|
CHC
|
B:HEC402
|
3.4
|
43.2
|
1.0
|
CHA
|
B:HEC402
|
3.4
|
40.4
|
1.0
|
CHB
|
B:HEC402
|
3.5
|
40.9
|
1.0
|
O
|
B:HOH597
|
3.9
|
46.9
|
1.0
|
CG
|
B:PRO107
|
4.1
|
48.5
|
1.0
|
CG
|
B:HIS35
|
4.2
|
41.2
|
1.0
|
ND1
|
B:HIS35
|
4.3
|
40.6
|
1.0
|
C2A
|
B:HEC402
|
4.4
|
40.1
|
1.0
|
C2C
|
B:HEC402
|
4.4
|
44.5
|
1.0
|
C3D
|
B:HEC402
|
4.4
|
41.0
|
1.0
|
C3C
|
B:HEC402
|
4.4
|
44.4
|
1.0
|
C2D
|
B:HEC402
|
4.4
|
41.9
|
1.0
|
C3A
|
B:HEC402
|
4.4
|
40.1
|
1.0
|
C3B
|
B:HEC402
|
4.4
|
42.3
|
1.0
|
C2B
|
B:HEC402
|
4.4
|
41.7
|
1.0
|
CB
|
B:PRO107
|
4.7
|
49.4
|
1.0
|
CG2
|
B:THR67
|
4.8
|
41.4
|
1.0
|
|
Iron binding site 4 out
of 4 in 4o1q
Go back to
Iron Binding Sites List in 4o1q
Iron binding site 4 out
of 4 in the Crystal Structure of the Q103N-Maug/Pre-Methylamine Dehydrogenase Complex
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 Q103N-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe403
b:36.7
occ:1.00
|
FE
|
B:HEC403
|
0.0
|
36.7
|
1.0
|
OH
|
B:TYR294
|
1.9
|
35.6
|
1.0
|
NB
|
B:HEC403
|
2.1
|
37.4
|
1.0
|
NA
|
B:HEC403
|
2.1
|
36.9
|
1.0
|
NC
|
B:HEC403
|
2.1
|
37.0
|
1.0
|
ND
|
B:HEC403
|
2.1
|
36.5
|
1.0
|
NE2
|
B:HIS205
|
2.3
|
36.9
|
1.0
|
CZ
|
B:TYR294
|
2.8
|
36.2
|
1.0
|
CD2
|
B:HIS205
|
3.0
|
37.3
|
1.0
|
C4B
|
B:HEC403
|
3.1
|
37.6
|
1.0
|
C4C
|
B:HEC403
|
3.1
|
36.8
|
1.0
|
C1D
|
B:HEC403
|
3.1
|
36.3
|
1.0
|
C1A
|
B:HEC403
|
3.1
|
36.9
|
1.0
|
C1B
|
B:HEC403
|
3.1
|
37.8
|
1.0
|
C4D
|
B:HEC403
|
3.1
|
36.4
|
1.0
|
C4A
|
B:HEC403
|
3.1
|
37.2
|
1.0
|
C1C
|
B:HEC403
|
3.1
|
37.3
|
1.0
|
CE1
|
B:HIS205
|
3.4
|
36.7
|
1.0
|
CHD
|
B:HEC403
|
3.4
|
36.6
|
1.0
|
CHC
|
B:HEC403
|
3.4
|
37.6
|
1.0
|
CHA
|
B:HEC403
|
3.4
|
36.6
|
1.0
|
CHB
|
B:HEC403
|
3.5
|
37.6
|
1.0
|
CE2
|
B:TYR294
|
3.5
|
36.7
|
1.0
|
CE1
|
B:TYR294
|
3.6
|
36.5
|
1.0
|
CG
|
B:HIS205
|
4.3
|
37.5
|
1.0
|
C3B
|
B:HEC403
|
4.4
|
38.4
|
1.0
|
C3C
|
B:HEC403
|
4.4
|
37.4
|
1.0
|
C3D
|
B:HEC403
|
4.4
|
36.3
|
1.0
|
C2D
|
B:HEC403
|
4.4
|
36.3
|
1.0
|
C2B
|
B:HEC403
|
4.4
|
38.5
|
1.0
|
C2A
|
B:HEC403
|
4.4
|
37.2
|
1.0
|
C3A
|
B:HEC403
|
4.4
|
37.5
|
1.0
|
ND1
|
B:HIS205
|
4.4
|
37.0
|
1.0
|
C2C
|
B:HEC403
|
4.4
|
37.6
|
1.0
|
CD2
|
B:TYR294
|
4.7
|
37.2
|
1.0
|
CD1
|
B:TYR294
|
4.8
|
36.9
|
1.0
|
|
Reference:
S.Shin,
E.T.Yukl,
E.Sehanobish,
C.M.Wilmot,
V.L.Davidson.
Site-Directed Mutagenesis of GLN103 Reveals the Influence of This Residue on the Redox Properties and Stability of Maug. Biochemistry V. 53 1342 2014.
ISSN: ISSN 0006-2960
PubMed: 24517455
DOI: 10.1021/BI5000349
Page generated: Mon Aug 5 08:04:23 2024
|