Iron in PDB 1fz1: Methane Monooxygenase Hydroxylase, Form III Oxidized
Enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Oxidized
All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Oxidized:
1.14.13.25;
Protein crystallography data
The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized, PDB code: 1fz1
was solved by
D.A.Whittington,
S.J.Lippard,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
22.80 /
1.96
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
71.400,
171.970,
221.380,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
20 /
23.4
|
Other elements in 1fz1:
The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form III Oxidized
(pdb code 1fz1). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the
Methane Monooxygenase Hydroxylase, Form III Oxidized, PDB code: 1fz1:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 1fz1
Go back to
Iron Binding Sites List in 1fz1
Iron binding site 1 out
of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 1 of Methane Monooxygenase Hydroxylase, Form III Oxidized within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe5001
b:25.7
occ:1.00
|
O
|
A:HOH9273
|
1.9
|
40.7
|
1.0
|
OE1
|
A:GLU114
|
2.0
|
27.9
|
1.0
|
ND1
|
A:HIS147
|
2.2
|
21.7
|
1.0
|
OE2
|
A:GLU144
|
2.2
|
25.2
|
1.0
|
O
|
A:HOH9187
|
2.4
|
24.8
|
1.0
|
O2
|
A:FMT9001
|
2.5
|
40.5
|
1.0
|
CD
|
A:GLU114
|
3.0
|
27.7
|
1.0
|
CE1
|
A:HIS147
|
3.1
|
21.3
|
1.0
|
CD
|
A:GLU144
|
3.1
|
23.0
|
1.0
|
FE
|
A:FE5002
|
3.2
|
36.7
|
1.0
|
CG
|
A:HIS147
|
3.3
|
20.2
|
1.0
|
C
|
A:FMT9001
|
3.3
|
45.0
|
1.0
|
OE1
|
A:GLU144
|
3.3
|
24.0
|
1.0
|
OE2
|
A:GLU114
|
3.4
|
29.6
|
1.0
|
CB
|
A:HIS147
|
3.6
|
18.5
|
1.0
|
O1
|
A:FMT9001
|
4.2
|
49.8
|
1.0
|
OE2
|
A:GLU243
|
4.2
|
48.4
|
1.0
|
NE2
|
A:HIS147
|
4.2
|
24.7
|
1.0
|
CD2
|
A:HIS147
|
4.3
|
23.9
|
1.0
|
CG
|
A:GLU114
|
4.4
|
25.0
|
1.0
|
CE1
|
A:HIS246
|
4.4
|
27.0
|
1.0
|
ND1
|
A:HIS246
|
4.5
|
27.7
|
1.0
|
CG
|
A:GLU144
|
4.6
|
17.5
|
1.0
|
OE1
|
A:GLU243
|
4.6
|
37.5
|
1.0
|
CB
|
A:GLU114
|
4.7
|
21.0
|
1.0
|
CA
|
A:GLU114
|
4.7
|
21.7
|
1.0
|
CA
|
A:GLU144
|
4.7
|
18.4
|
1.0
|
OE2
|
A:GLU209
|
4.7
|
46.7
|
1.0
|
CG2
|
A:ILE239
|
4.8
|
22.5
|
1.0
|
CD
|
A:GLU243
|
4.8
|
42.6
|
1.0
|
|
Iron binding site 2 out
of 4 in 1fz1
Go back to
Iron Binding Sites List in 1fz1
Iron binding site 2 out
of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 2 of Methane Monooxygenase Hydroxylase, Form III Oxidized within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe5002
b:36.7
occ:1.00
|
OE2
|
A:GLU209
|
2.0
|
46.7
|
1.0
|
O
|
A:HOH9273
|
2.0
|
40.7
|
1.0
|
ND1
|
A:HIS246
|
2.2
|
27.7
|
1.0
|
OE1
|
A:GLU243
|
2.4
|
37.5
|
1.0
|
OE1
|
A:GLU144
|
2.4
|
24.0
|
1.0
|
O2
|
A:FMT9001
|
2.5
|
40.5
|
1.0
|
CE1
|
A:HIS246
|
3.0
|
27.0
|
1.0
|
CD
|
A:GLU209
|
3.1
|
46.8
|
1.0
|
CD
|
A:GLU243
|
3.2
|
42.6
|
1.0
|
FE
|
A:FE5001
|
3.2
|
25.7
|
1.0
|
OE2
|
A:GLU243
|
3.3
|
48.4
|
1.0
|
CG
|
A:HIS246
|
3.3
|
28.4
|
1.0
|
CD
|
A:GLU144
|
3.4
|
23.0
|
1.0
|
OE2
|
A:GLU144
|
3.7
|
25.2
|
1.0
|
C
|
A:FMT9001
|
3.7
|
45.0
|
1.0
|
CB
|
A:HIS246
|
3.8
|
30.0
|
1.0
|
NE2
|
A:GLN140
|
3.9
|
26.3
|
1.0
|
OE1
|
A:GLU209
|
3.9
|
47.6
|
1.0
|
CG
|
A:GLU209
|
4.0
|
45.9
|
1.0
|
NE2
|
A:HIS246
|
4.2
|
27.9
|
1.0
|
O
|
A:HOH9187
|
4.3
|
24.8
|
1.0
|
CD2
|
A:HIS246
|
4.4
|
26.9
|
1.0
|
O1
|
A:FMT9001
|
4.5
|
49.8
|
1.0
|
CD
|
A:GLN140
|
4.5
|
26.5
|
1.0
|
CG
|
A:GLU243
|
4.6
|
40.4
|
1.0
|
ND1
|
A:HIS147
|
4.6
|
21.7
|
1.0
|
CE1
|
A:HIS147
|
4.6
|
21.3
|
1.0
|
CG
|
A:GLN140
|
4.7
|
25.5
|
1.0
|
CG
|
A:GLU144
|
4.8
|
17.5
|
1.0
|
CB
|
A:GLU209
|
4.9
|
42.4
|
1.0
|
OE1
|
A:GLU114
|
5.0
|
27.9
|
1.0
|
|
Iron binding site 3 out
of 4 in 1fz1
Go back to
Iron Binding Sites List in 1fz1
Iron binding site 3 out
of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 3 of Methane Monooxygenase Hydroxylase, Form III Oxidized within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe5003
b:26.0
occ:1.00
|
O
|
B:HOH5170
|
1.8
|
35.7
|
1.0
|
OE1
|
B:GLU114
|
2.0
|
25.6
|
1.0
|
OE2
|
B:GLU144
|
2.2
|
24.9
|
1.0
|
ND1
|
B:HIS147
|
2.2
|
18.9
|
1.0
|
O
|
B:HOH5169
|
2.4
|
31.9
|
1.0
|
O
|
B:HOH5293
|
2.7
|
36.4
|
1.0
|
CD
|
B:GLU114
|
2.9
|
26.8
|
1.0
|
CD
|
B:GLU144
|
3.1
|
23.2
|
1.0
|
CE1
|
B:HIS147
|
3.1
|
17.1
|
1.0
|
FE
|
B:FE5004
|
3.2
|
36.6
|
1.0
|
CG
|
B:HIS147
|
3.2
|
14.3
|
1.0
|
OE2
|
B:GLU114
|
3.3
|
32.9
|
1.0
|
OE1
|
B:GLU144
|
3.4
|
27.6
|
1.0
|
CB
|
B:HIS147
|
3.6
|
19.5
|
1.0
|
OE2
|
B:GLU243
|
4.2
|
48.0
|
1.0
|
NE2
|
B:HIS147
|
4.3
|
21.0
|
1.0
|
CG
|
B:GLU114
|
4.3
|
23.0
|
1.0
|
CD2
|
B:HIS147
|
4.3
|
17.0
|
1.0
|
CE1
|
B:HIS246
|
4.4
|
32.3
|
1.0
|
ND1
|
B:HIS246
|
4.5
|
29.6
|
1.0
|
CG
|
B:GLU144
|
4.5
|
22.0
|
1.0
|
CA
|
B:GLU144
|
4.6
|
19.3
|
1.0
|
CB
|
B:GLU114
|
4.6
|
22.1
|
1.0
|
O
|
B:HOH5294
|
4.7
|
45.1
|
1.0
|
OE1
|
B:GLU243
|
4.7
|
40.6
|
1.0
|
CA
|
B:GLU114
|
4.7
|
21.7
|
1.0
|
CG2
|
B:ILE239
|
4.8
|
20.2
|
1.0
|
OE1
|
B:GLU209
|
4.8
|
42.6
|
1.0
|
CD
|
B:GLU243
|
4.8
|
45.3
|
1.0
|
CB
|
B:GLU144
|
4.9
|
18.4
|
1.0
|
|
Iron binding site 4 out
of 4 in 1fz1
Go back to
Iron Binding Sites List in 1fz1
Iron binding site 4 out
of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized
Mono view
Stereo pair view
|
A full contact list of Iron with other atoms in the Fe binding
site number 4 of Methane Monooxygenase Hydroxylase, Form III Oxidized within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe5004
b:36.6
occ:1.00
|
O
|
B:HOH5170
|
1.9
|
35.7
|
1.0
|
ND1
|
B:HIS246
|
2.2
|
29.6
|
1.0
|
OE1
|
B:GLU209
|
2.2
|
42.6
|
1.0
|
OE1
|
B:GLU243
|
2.3
|
40.6
|
1.0
|
OE1
|
B:GLU144
|
2.5
|
27.6
|
1.0
|
O
|
B:HOH5293
|
2.8
|
36.4
|
1.0
|
CE1
|
B:HIS246
|
3.0
|
32.3
|
1.0
|
CD
|
B:GLU209
|
3.0
|
45.3
|
1.0
|
CD
|
B:GLU243
|
3.1
|
45.3
|
1.0
|
FE
|
B:FE5003
|
3.2
|
26.0
|
1.0
|
OE2
|
B:GLU243
|
3.3
|
48.0
|
1.0
|
CG
|
B:HIS246
|
3.3
|
29.7
|
1.0
|
CD
|
B:GLU144
|
3.4
|
23.2
|
1.0
|
OE2
|
B:GLU144
|
3.6
|
24.9
|
1.0
|
CG
|
B:GLU209
|
3.7
|
43.5
|
1.0
|
NE2
|
B:GLN140
|
3.7
|
22.9
|
1.0
|
CB
|
B:HIS246
|
3.8
|
29.6
|
1.0
|
OE2
|
B:GLU209
|
3.8
|
46.0
|
1.0
|
O
|
B:HOH5169
|
4.1
|
31.9
|
1.0
|
NE2
|
B:HIS246
|
4.2
|
29.9
|
1.0
|
CD2
|
B:HIS246
|
4.4
|
29.7
|
1.0
|
CD
|
B:GLN140
|
4.5
|
28.9
|
1.0
|
ND1
|
B:HIS147
|
4.5
|
18.9
|
1.0
|
CG
|
B:GLU243
|
4.6
|
41.7
|
1.0
|
CE1
|
B:HIS147
|
4.6
|
17.1
|
1.0
|
CG
|
B:GLN140
|
4.7
|
24.8
|
1.0
|
CG
|
B:GLU144
|
4.8
|
22.0
|
1.0
|
OE1
|
B:GLU114
|
4.9
|
25.6
|
1.0
|
O
|
B:HOH5294
|
4.9
|
45.1
|
1.0
|
CB
|
B:GLU209
|
4.9
|
43.3
|
1.0
|
|
Reference:
D.A.Whittington,
S.J.Lippard.
Crystal Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) Demonstrating Geometrical Variability at the Dinuclear Iron Active Site. J.Am.Chem.Soc. V. 123 827 2001.
ISSN: ISSN 0002-7863
PubMed: 11456616
DOI: 10.1021/JA003240N
Page generated: Sat Aug 3 05:32:25 2024
|