Iron in PDB 3rn0: Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex
Enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex
All present enzymatic activity of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex:
1.4.99.3;
Protein crystallography data
The structure of Crystal Structure of the W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0
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)
|
39.58 /
1.91
|
Space group
|
P 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
55.527,
83.524,
107.782,
109.94,
91.54,
105.78
|
R / Rfree (%)
|
17.3 /
23
|
Other elements in 3rn0:
The structure of Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex
(pdb code 3rn0). 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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex, PDB code: 3rn0:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 3rn0
Go back to
Iron Binding Sites List in 3rn0
Iron binding site 1 out
of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe500
b:31.7
occ:1.00
|
FE
|
A:HEC500
|
0.0
|
31.7
|
1.0
|
NE2
|
A:HIS35
|
2.0
|
28.6
|
1.0
|
NC
|
A:HEC500
|
2.1
|
33.3
|
1.0
|
ND
|
A:HEC500
|
2.1
|
29.3
|
1.0
|
NB
|
A:HEC500
|
2.1
|
30.6
|
1.0
|
NA
|
A:HEC500
|
2.1
|
33.7
|
1.0
|
CD2
|
A:HIS35
|
2.9
|
31.6
|
1.0
|
CE1
|
A:HIS35
|
3.0
|
29.5
|
1.0
|
C1D
|
A:HEC500
|
3.1
|
31.2
|
1.0
|
C4C
|
A:HEC500
|
3.1
|
35.3
|
1.0
|
C1C
|
A:HEC500
|
3.1
|
29.5
|
1.0
|
C4B
|
A:HEC500
|
3.1
|
33.3
|
1.0
|
C4D
|
A:HEC500
|
3.1
|
32.3
|
1.0
|
C1B
|
A:HEC500
|
3.1
|
33.3
|
1.0
|
C4A
|
A:HEC500
|
3.1
|
32.1
|
1.0
|
C1A
|
A:HEC500
|
3.1
|
29.8
|
1.0
|
O
|
A:HOH437
|
3.2
|
21.8
|
1.0
|
CHD
|
A:HEC500
|
3.4
|
28.9
|
1.0
|
CHB
|
A:HEC500
|
3.5
|
28.8
|
1.0
|
CHC
|
A:HEC500
|
3.5
|
29.9
|
1.0
|
CHA
|
A:HEC500
|
3.5
|
27.1
|
1.0
|
NE2
|
A:GLN103
|
4.1
|
30.5
|
1.0
|
ND1
|
A:HIS35
|
4.1
|
30.0
|
1.0
|
CG
|
A:HIS35
|
4.1
|
27.8
|
1.0
|
CG
|
A:PRO107
|
4.2
|
37.0
|
1.0
|
C2D
|
A:HEC500
|
4.4
|
29.0
|
1.0
|
C2C
|
A:HEC500
|
4.4
|
30.3
|
1.0
|
C3D
|
A:HEC500
|
4.4
|
30.6
|
1.0
|
C3C
|
A:HEC500
|
4.4
|
29.2
|
1.0
|
C3B
|
A:HEC500
|
4.4
|
33.5
|
1.0
|
C2B
|
A:HEC500
|
4.4
|
31.1
|
1.0
|
C3A
|
A:HEC500
|
4.4
|
31.2
|
1.0
|
C2A
|
A:HEC500
|
4.4
|
30.6
|
1.0
|
CB
|
A:PRO107
|
4.8
|
37.2
|
1.0
|
|
Iron binding site 2 out
of 4 in 3rn0
Go back to
Iron Binding Sites List in 3rn0
Iron binding site 2 out
of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe600
b:28.6
occ:1.00
|
FE
|
A:HEC600
|
0.0
|
28.6
|
1.0
|
NB
|
A:HEC600
|
2.0
|
25.3
|
1.0
|
NE2
|
A:HIS205
|
2.0
|
26.4
|
1.0
|
OH
|
A:TYR294
|
2.1
|
30.7
|
1.0
|
NC
|
A:HEC600
|
2.1
|
25.6
|
1.0
|
ND
|
A:HEC600
|
2.1
|
25.0
|
1.0
|
NA
|
A:HEC600
|
2.1
|
25.1
|
1.0
|
CZ
|
A:TYR294
|
2.9
|
31.7
|
1.0
|
C1B
|
A:HEC600
|
3.0
|
29.6
|
1.0
|
CE1
|
A:HIS205
|
3.0
|
27.4
|
1.0
|
CD2
|
A:HIS205
|
3.0
|
28.1
|
1.0
|
C4B
|
A:HEC600
|
3.0
|
30.7
|
1.0
|
C1A
|
A:HEC600
|
3.1
|
24.2
|
1.0
|
C1C
|
A:HEC600
|
3.1
|
26.9
|
1.0
|
C1D
|
A:HEC600
|
3.1
|
28.4
|
1.0
|
C4D
|
A:HEC600
|
3.1
|
26.8
|
1.0
|
C4C
|
A:HEC600
|
3.1
|
29.1
|
1.0
|
C4A
|
A:HEC600
|
3.1
|
28.3
|
1.0
|
CHB
|
A:HEC600
|
3.4
|
28.6
|
1.0
|
CHC
|
A:HEC600
|
3.4
|
27.5
|
1.0
|
CHA
|
A:HEC600
|
3.4
|
18.5
|
1.0
|
CHD
|
A:HEC600
|
3.4
|
27.3
|
1.0
|
CE1
|
A:TYR294
|
3.6
|
27.2
|
1.0
|
CE2
|
A:TYR294
|
3.8
|
25.7
|
1.0
|
ND1
|
A:HIS205
|
4.1
|
30.6
|
1.0
|
CG
|
A:HIS205
|
4.2
|
29.1
|
1.0
|
C2B
|
A:HEC600
|
4.3
|
29.2
|
1.0
|
C3B
|
A:HEC600
|
4.3
|
28.5
|
1.0
|
C3D
|
A:HEC600
|
4.4
|
28.4
|
1.0
|
C2A
|
A:HEC600
|
4.4
|
28.6
|
1.0
|
C2D
|
A:HEC600
|
4.4
|
25.7
|
1.0
|
C2C
|
A:HEC600
|
4.4
|
28.9
|
1.0
|
C3C
|
A:HEC600
|
4.4
|
24.5
|
1.0
|
C3A
|
A:HEC600
|
4.4
|
28.0
|
1.0
|
CD1
|
A:TYR294
|
4.9
|
29.2
|
1.0
|
CD2
|
A:TYR294
|
4.9
|
26.6
|
1.0
|
|
Iron binding site 3 out
of 4 in 3rn0
Go back to
Iron Binding Sites List in 3rn0
Iron binding site 3 out
of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe500
b:25.9
occ:1.00
|
FE
|
B:HEC500
|
0.0
|
25.9
|
1.0
|
NC
|
B:HEC500
|
2.1
|
27.2
|
1.0
|
NE2
|
B:HIS35
|
2.1
|
24.0
|
1.0
|
NA
|
B:HEC500
|
2.1
|
26.9
|
1.0
|
NB
|
B:HEC500
|
2.1
|
26.5
|
1.0
|
ND
|
B:HEC500
|
2.1
|
26.2
|
1.0
|
O
|
B:HOH1182
|
2.4
|
36.5
|
1.0
|
C4C
|
B:HEC500
|
3.0
|
24.0
|
1.0
|
CE1
|
B:HIS35
|
3.0
|
22.7
|
1.0
|
C1C
|
B:HEC500
|
3.0
|
24.7
|
1.0
|
C1A
|
B:HEC500
|
3.0
|
21.1
|
1.0
|
C4A
|
B:HEC500
|
3.1
|
24.3
|
1.0
|
C4B
|
B:HEC500
|
3.1
|
27.5
|
1.0
|
CD2
|
B:HIS35
|
3.1
|
24.8
|
1.0
|
C1D
|
B:HEC500
|
3.1
|
23.6
|
1.0
|
C1B
|
B:HEC500
|
3.1
|
26.4
|
1.0
|
C4D
|
B:HEC500
|
3.1
|
20.0
|
1.0
|
CHD
|
B:HEC500
|
3.4
|
23.5
|
1.0
|
CHC
|
B:HEC500
|
3.4
|
19.6
|
1.0
|
CHA
|
B:HEC500
|
3.4
|
19.1
|
1.0
|
CHB
|
B:HEC500
|
3.4
|
22.8
|
1.0
|
O
|
B:HOH407
|
4.0
|
35.8
|
1.0
|
NE2
|
B:GLN103
|
4.1
|
24.9
|
1.0
|
ND1
|
B:HIS35
|
4.2
|
23.0
|
1.0
|
CG
|
B:HIS35
|
4.2
|
23.6
|
1.0
|
CG
|
B:PRO107
|
4.3
|
27.3
|
1.0
|
C3C
|
B:HEC500
|
4.3
|
24.6
|
1.0
|
C2C
|
B:HEC500
|
4.3
|
21.0
|
1.0
|
C2A
|
B:HEC500
|
4.4
|
22.9
|
1.0
|
C3A
|
B:HEC500
|
4.4
|
22.9
|
1.0
|
C3B
|
B:HEC500
|
4.4
|
24.4
|
1.0
|
C2D
|
B:HEC500
|
4.4
|
25.3
|
1.0
|
C2B
|
B:HEC500
|
4.4
|
27.0
|
1.0
|
C3D
|
B:HEC500
|
4.4
|
24.5
|
1.0
|
CB
|
B:PRO107
|
5.0
|
29.3
|
1.0
|
|
Iron binding site 4 out
of 4 in 3rn0
Go back to
Iron Binding Sites List in 3rn0
Iron binding site 4 out
of 4 in the Crystal Structure of the W199K-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 W199K-Maug/Pre-Methylamine Dehydrogenase Complex within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe600
b:20.2
occ:1.00
|
FE
|
B:HEC600
|
0.0
|
20.2
|
1.0
|
OH
|
B:TYR294
|
1.9
|
19.0
|
1.0
|
NC
|
B:HEC600
|
2.0
|
18.5
|
1.0
|
NB
|
B:HEC600
|
2.1
|
17.4
|
1.0
|
NA
|
B:HEC600
|
2.1
|
21.4
|
1.0
|
ND
|
B:HEC600
|
2.1
|
21.0
|
1.0
|
NE2
|
B:HIS205
|
2.1
|
19.4
|
1.0
|
CD2
|
B:HIS205
|
2.9
|
21.7
|
1.0
|
CZ
|
B:TYR294
|
3.0
|
19.1
|
1.0
|
C1D
|
B:HEC600
|
3.0
|
17.2
|
1.0
|
C1A
|
B:HEC600
|
3.0
|
19.6
|
1.0
|
C1C
|
B:HEC600
|
3.0
|
15.2
|
1.0
|
C4C
|
B:HEC600
|
3.0
|
14.8
|
1.0
|
C4B
|
B:HEC600
|
3.0
|
16.3
|
1.0
|
C4D
|
B:HEC600
|
3.1
|
18.5
|
1.0
|
C1B
|
B:HEC600
|
3.1
|
16.7
|
1.0
|
C4A
|
B:HEC600
|
3.1
|
22.2
|
1.0
|
CE1
|
B:HIS205
|
3.2
|
15.5
|
1.0
|
CHD
|
B:HEC600
|
3.3
|
14.6
|
1.0
|
CHA
|
B:HEC600
|
3.4
|
15.6
|
1.0
|
CHC
|
B:HEC600
|
3.4
|
12.2
|
1.0
|
CHB
|
B:HEC600
|
3.4
|
20.1
|
1.0
|
CE1
|
B:TYR294
|
3.7
|
24.0
|
1.0
|
CE2
|
B:TYR294
|
3.8
|
22.2
|
1.0
|
CG
|
B:HIS205
|
4.1
|
23.2
|
1.0
|
ND1
|
B:HIS205
|
4.2
|
19.7
|
1.0
|
C2D
|
B:HEC600
|
4.3
|
18.3
|
1.0
|
C2C
|
B:HEC600
|
4.3
|
18.1
|
1.0
|
C2A
|
B:HEC600
|
4.3
|
18.5
|
1.0
|
C3C
|
B:HEC600
|
4.3
|
13.5
|
1.0
|
C3D
|
B:HEC600
|
4.3
|
17.9
|
1.0
|
C3B
|
B:HEC600
|
4.3
|
15.5
|
1.0
|
C2B
|
B:HEC600
|
4.3
|
19.3
|
1.0
|
C3A
|
B:HEC600
|
4.4
|
20.1
|
1.0
|
CD1
|
B:TYR294
|
4.9
|
19.9
|
1.0
|
|
Reference:
N.A.Tarboush,
L.M.Jensen,
E.T.Yukl,
J.Geng,
A.Liu,
C.M.Wilmot,
V.L.Davidson.
Mutagenesis of TRYPTOPHAN199 Suggests That Hopping Is Required For Maug-Dependent Tryptophan Tryptophylquinone Biosynthesis. Proc.Natl.Acad.Sci.Usa V. 108 16956 2011.
ISSN: ISSN 0027-8424
PubMed: 21969534
DOI: 10.1073/PNAS.1109423108
Page generated: Sun Aug 4 19:41:46 2024
|