Iron in PDB 1xvd: Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
Enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
All present enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure:
1.14.13.25;
Protein crystallography data
The structure of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure, PDB code: 1xvd
was solved by
M.H.Sazinsky,
S.J.Lippard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
29.94 /
2.30
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
71.182,
171.497,
221.304,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
19.4 /
22.9
|
Other elements in 1xvd:
The structure of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
(pdb code 1xvd). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure, PDB code: 1xvd:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1xvd
Go back to
Iron Binding Sites List in 1xvd
Iron binding site 1 out
of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe528
b:63.1
occ:1.00
|
OE1
|
A:GLU114
|
2.1
|
61.1
|
1.0
|
ND1
|
A:HIS147
|
2.3
|
34.7
|
1.0
|
OE2
|
A:GLU144
|
2.7
|
42.3
|
1.0
|
FE
|
A:FE529
|
2.8
|
78.5
|
1.0
|
CD
|
A:GLU114
|
2.9
|
58.6
|
1.0
|
O
|
A:HOH2862
|
2.9
|
52.4
|
1.0
|
OE2
|
A:GLU114
|
2.9
|
61.7
|
1.0
|
CE1
|
A:HIS147
|
3.0
|
34.7
|
1.0
|
O
|
A:HOH2861
|
3.2
|
47.1
|
1.0
|
OE1
|
A:GLU144
|
3.4
|
44.0
|
1.0
|
CD
|
A:GLU144
|
3.4
|
40.9
|
1.0
|
CG
|
A:HIS147
|
3.5
|
32.8
|
1.0
|
CE1
|
A:HIS246
|
3.9
|
66.9
|
1.0
|
OE2
|
A:GLU243
|
3.9
|
62.8
|
1.0
|
ND1
|
A:HIS246
|
4.0
|
66.8
|
1.0
|
CB
|
A:HIS147
|
4.0
|
31.0
|
1.0
|
NE2
|
A:HIS147
|
4.2
|
33.6
|
1.0
|
CG
|
A:GLU114
|
4.4
|
53.3
|
1.0
|
CD2
|
A:HIS147
|
4.5
|
34.5
|
1.0
|
OE1
|
A:GLU243
|
4.5
|
64.5
|
1.0
|
CD
|
A:GLU243
|
4.6
|
63.7
|
1.0
|
CG2
|
A:ILE239
|
4.7
|
38.7
|
1.0
|
OE2
|
A:GLU209
|
4.7
|
71.2
|
1.0
|
CB
|
A:GLU114
|
4.9
|
45.8
|
1.0
|
CG
|
A:GLU144
|
4.9
|
40.7
|
1.0
|
|
Iron binding site 2 out
of 4 in 1xvd
Go back to
Iron Binding Sites List in 1xvd
Iron binding site 2 out
of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe529
b:78.5
occ:1.00
|
ND1
|
A:HIS246
|
2.1
|
66.8
|
1.0
|
OE2
|
A:GLU209
|
2.4
|
71.2
|
1.0
|
OE1
|
A:GLU243
|
2.6
|
64.5
|
1.0
|
FE
|
A:FE528
|
2.8
|
63.1
|
1.0
|
OE2
|
A:GLU243
|
2.8
|
62.8
|
1.0
|
CE1
|
A:HIS246
|
2.9
|
66.9
|
1.0
|
OE1
|
A:GLU144
|
3.0
|
44.0
|
1.0
|
CD
|
A:GLU243
|
3.1
|
63.7
|
1.0
|
CG
|
A:HIS246
|
3.2
|
66.1
|
1.0
|
CD
|
A:GLU209
|
3.3
|
71.5
|
1.0
|
O
|
A:HOH2861
|
3.5
|
47.1
|
1.0
|
CB
|
A:HIS246
|
3.6
|
63.8
|
1.0
|
NE2
|
A:GLN140
|
3.7
|
42.2
|
1.0
|
CD
|
A:GLU144
|
3.9
|
40.9
|
1.0
|
O
|
A:HOH2862
|
4.0
|
52.4
|
1.0
|
OE2
|
A:GLU144
|
4.1
|
42.3
|
1.0
|
NE2
|
A:HIS246
|
4.1
|
67.0
|
1.0
|
CG
|
A:GLU209
|
4.1
|
70.1
|
1.0
|
OE1
|
A:GLU209
|
4.1
|
73.5
|
1.0
|
CD2
|
A:HIS246
|
4.2
|
65.6
|
1.0
|
CE1
|
A:HIS147
|
4.5
|
34.7
|
1.0
|
ND1
|
A:HIS147
|
4.5
|
34.7
|
1.0
|
CD
|
A:GLN140
|
4.5
|
43.8
|
1.0
|
CG
|
A:GLU243
|
4.5
|
61.9
|
1.0
|
OE1
|
A:GLU114
|
4.8
|
61.1
|
1.0
|
CG
|
A:GLN140
|
4.8
|
43.0
|
1.0
|
CB
|
A:GLU209
|
4.9
|
67.2
|
1.0
|
|
Iron binding site 3 out
of 4 in 1xvd
Go back to
Iron Binding Sites List in 1xvd
Iron binding site 3 out
of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe528
b:63.0
occ:1.00
|
OE1
|
B:GLU114
|
1.9
|
55.6
|
1.0
|
ND1
|
B:HIS147
|
2.2
|
35.5
|
1.0
|
OE2
|
B:GLU144
|
2.4
|
44.0
|
1.0
|
FE
|
B:FE529
|
2.6
|
72.9
|
1.0
|
O
|
B:HOH2864
|
2.7
|
55.6
|
1.0
|
CD
|
B:GLU114
|
2.9
|
51.0
|
1.0
|
O
|
B:HOH2865
|
2.9
|
45.9
|
1.0
|
CE1
|
B:HIS147
|
3.0
|
36.4
|
1.0
|
OE2
|
B:GLU114
|
3.2
|
55.4
|
1.0
|
CD
|
B:GLU144
|
3.2
|
42.3
|
1.0
|
CG
|
B:HIS147
|
3.3
|
33.7
|
1.0
|
OE1
|
B:GLU144
|
3.3
|
42.3
|
1.0
|
CE1
|
B:HIS246
|
3.6
|
66.9
|
1.0
|
CB
|
B:HIS147
|
3.7
|
32.9
|
1.0
|
ND1
|
B:HIS246
|
3.9
|
66.6
|
1.0
|
OE2
|
B:GLU243
|
4.1
|
62.4
|
1.0
|
NE2
|
B:HIS147
|
4.2
|
36.3
|
1.0
|
CG
|
B:GLU114
|
4.2
|
48.3
|
1.0
|
OE1
|
B:GLU243
|
4.4
|
63.2
|
1.0
|
CD2
|
B:HIS147
|
4.4
|
34.1
|
1.0
|
CD
|
B:GLU243
|
4.7
|
62.3
|
1.0
|
CG
|
B:GLU144
|
4.7
|
40.5
|
1.0
|
CB
|
B:GLU114
|
4.7
|
42.9
|
1.0
|
OE1
|
B:GLU209
|
4.8
|
68.2
|
1.0
|
CA
|
B:GLU144
|
4.8
|
37.2
|
1.0
|
CG2
|
B:ILE239
|
4.8
|
36.7
|
1.0
|
NE2
|
B:HIS246
|
4.9
|
65.8
|
1.0
|
CA
|
B:GLU114
|
4.9
|
40.9
|
1.0
|
|
Iron binding site 4 out
of 4 in 1xvd
Go back to
Iron Binding Sites List in 1xvd
Iron binding site 4 out
of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe529
b:72.9
occ:1.00
|
ND1
|
B:HIS246
|
1.9
|
66.6
|
1.0
|
OE1
|
B:GLU243
|
2.5
|
63.2
|
1.0
|
CE1
|
B:HIS246
|
2.5
|
66.9
|
1.0
|
FE
|
B:FE528
|
2.6
|
63.0
|
1.0
|
OE1
|
B:GLU144
|
2.7
|
42.3
|
1.0
|
OE1
|
B:GLU209
|
2.7
|
68.2
|
1.0
|
O
|
B:HOH2864
|
3.1
|
55.6
|
1.0
|
OE2
|
B:GLU243
|
3.2
|
62.4
|
1.0
|
CG
|
B:HIS246
|
3.2
|
65.6
|
1.0
|
CD
|
B:GLU243
|
3.2
|
62.3
|
1.0
|
CD
|
B:GLU209
|
3.4
|
68.7
|
1.0
|
O
|
B:HOH2865
|
3.4
|
45.9
|
1.0
|
CD
|
B:GLU144
|
3.5
|
42.3
|
1.0
|
OE2
|
B:GLU144
|
3.6
|
44.0
|
1.0
|
NE2
|
B:HIS246
|
3.8
|
65.8
|
1.0
|
CB
|
B:HIS246
|
3.9
|
64.1
|
1.0
|
OE2
|
B:GLU209
|
4.1
|
67.4
|
1.0
|
CD2
|
B:HIS246
|
4.1
|
66.0
|
1.0
|
CG
|
B:GLU209
|
4.1
|
68.8
|
1.0
|
ND1
|
B:HIS147
|
4.1
|
35.5
|
1.0
|
CE1
|
B:HIS147
|
4.2
|
36.4
|
1.0
|
OE1
|
B:GLU114
|
4.3
|
55.6
|
1.0
|
NE2
|
B:GLN140
|
4.4
|
49.4
|
1.0
|
CG
|
B:GLU243
|
4.7
|
60.4
|
1.0
|
CD
|
B:GLN140
|
4.7
|
48.8
|
1.0
|
CG
|
B:GLN140
|
4.9
|
47.8
|
1.0
|
CG
|
B:GLU144
|
5.0
|
40.5
|
1.0
|
|
Reference:
M.H.Sazinsky,
S.J.Lippard.
Product Bound Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath): Protein Motion in the Alpha-Subunit J.Am.Chem.Soc. V. 127 5814 2005.
ISSN: ISSN 0002-7863
PubMed: 15839679
DOI: 10.1021/JA044099B
Page generated: Sat Aug 3 17:04:12 2024
|