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Iron in PDB 1fz6: Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol, PDB code: 1fz6 was solved by D.A.Whittington, 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) 29.90 / 2.05
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.670, 171.290, 221.340, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 24.4

Other elements in 1fz6:

The structure of Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol (pdb code 1fz6). 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 II Soaked in 1 M Methanol, PDB code: 1fz6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz6

Go back to Iron Binding Sites List in 1fz6
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:30.5
occ:1.00
O A:HOH5219 1.9 51.3 1.0
OE1 A:GLU114 2.1 32.2 1.0
O A:HOH5218 2.2 41.9 1.0
OE2 A:GLU144 2.2 29.1 1.0
ND1 A:HIS147 2.2 24.3 1.0
O A:HOH5217 2.4 41.8 1.0
FE A:FE5002 3.0 42.3 1.0
CE1 A:HIS147 3.1 24.4 1.0
CD A:GLU114 3.1 33.3 1.0
CD A:GLU144 3.2 29.2 1.0
CG A:HIS147 3.3 23.9 1.0
OE2 A:GLU114 3.4 36.4 1.0
OE1 A:GLU144 3.5 30.1 1.0
CB A:HIS147 3.7 23.4 1.0
OE2 A:GLU243 3.9 48.0 1.0
O A:HOH5220 4.0 60.0 1.0
CE1 A:HIS246 4.2 38.4 1.0
NE2 A:HIS147 4.3 25.1 1.0
OE1 A:GLU243 4.3 43.7 1.0
CD2 A:HIS147 4.4 24.8 1.0
ND1 A:HIS246 4.4 37.8 1.0
OE2 A:GLU209 4.4 45.6 1.0
CG A:GLU114 4.5 32.0 1.0
CD A:GLU243 4.5 45.6 1.0
CG A:GLU144 4.6 28.3 1.0
CG2 A:ILE239 4.7 27.0 1.0
CB A:GLU114 4.8 28.2 1.0
CA A:GLU144 4.8 26.0 1.0
CA A:GLU114 4.8 28.1 1.0

Iron binding site 2 out of 4 in 1fz6

Go back to Iron Binding Sites List in 1fz6
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:42.3
occ:1.00
O A:HOH5219 1.9 51.3 1.0
OE2 A:GLU209 1.9 45.6 1.0
O A:HOH5218 2.2 41.9 1.0
ND1 A:HIS246 2.2 37.8 1.0
OE1 A:GLU243 2.2 43.7 1.0
OE1 A:GLU144 2.5 30.1 1.0
CE1 A:HIS246 3.0 38.4 1.0
CD A:GLU243 3.0 45.6 1.0
FE A:FE5001 3.0 30.5 1.0
CD A:GLU209 3.0 45.2 1.0
OE2 A:GLU243 3.1 48.0 1.0
CG A:HIS246 3.3 37.4 1.0
CD A:GLU144 3.4 29.2 1.0
OE2 A:GLU144 3.5 29.1 1.0
OE1 A:GLU209 3.8 45.6 1.0
CB A:HIS246 3.8 39.1 1.0
NE2 A:GLN140 3.9 27.3 1.0
CG A:GLU209 3.9 44.5 1.0
NE2 A:HIS246 4.2 35.9 1.0
O A:HOH5217 4.2 41.8 1.0
CD2 A:HIS246 4.4 36.0 1.0
CG A:GLU243 4.4 43.6 1.0
ND1 A:HIS147 4.5 24.3 1.0
CE1 A:HIS147 4.6 24.4 1.0
CD A:GLN140 4.6 31.2 1.0
O A:HOH5220 4.7 60.0 1.0
CG A:GLN140 4.8 29.8 1.0
CG A:GLU144 4.8 28.3 1.0
OE1 A:GLU114 4.8 32.2 1.0
CB A:GLU209 4.9 41.9 1.0

Iron binding site 3 out of 4 in 1fz6

Go back to Iron Binding Sites List in 1fz6
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:30.8
occ:1.00
OE1 B:GLU114 1.9 31.9 1.0
O B:HOH9198 1.9 37.8 1.0
O B:MOH9001 2.1 45.1 1.0
ND1 B:HIS147 2.1 23.3 1.0
OE2 B:GLU144 2.2 29.6 1.0
O B:HOH9197 2.3 35.9 1.0
CD B:GLU114 2.9 30.4 1.0
C B:MOH9001 3.0 43.6 1.0
FE B:FE5004 3.0 41.2 1.0
CE1 B:HIS147 3.0 22.7 1.0
CG B:HIS147 3.1 21.9 1.0
CD B:GLU144 3.2 28.6 1.0
OE2 B:GLU114 3.2 34.3 1.0
OE1 B:GLU144 3.4 29.9 1.0
CB B:HIS147 3.5 22.9 1.0
NE2 B:HIS147 4.2 25.2 1.0
OE2 B:GLU243 4.2 51.0 1.0
CD2 B:HIS147 4.2 22.0 1.0
CG B:GLU114 4.3 30.6 1.0
CE1 B:HIS246 4.4 39.9 1.0
OE1 B:GLU243 4.4 46.5 1.0
ND1 B:HIS246 4.5 41.0 1.0
CG2 B:ILE239 4.6 27.6 1.0
CG B:GLU144 4.6 27.2 1.0
OE1 B:GLU209 4.6 42.1 1.0
CA B:GLU144 4.6 25.3 1.0
CB B:GLU114 4.6 28.9 1.0
CD B:GLU243 4.7 49.0 1.0
CA B:GLU114 4.7 30.1 1.0
CB B:GLU144 5.0 24.5 1.0

Iron binding site 4 out of 4 in 1fz6

Go back to Iron Binding Sites List in 1fz6
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Soaked in 1 M Methanol


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 II Soaked in 1 M Methanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:41.2
occ:1.00
O B:HOH9198 1.9 37.8 1.0
OE1 B:GLU209 2.0 42.1 1.0
O B:MOH9001 2.1 45.1 1.0
ND1 B:HIS246 2.2 41.0 1.0
OE1 B:GLU243 2.3 46.5 1.0
OE1 B:GLU144 2.4 29.9 1.0
CE1 B:HIS246 3.0 39.9 1.0
FE B:FE5003 3.0 30.8 1.0
CD B:GLU209 3.0 41.3 1.0
CD B:GLU144 3.3 28.6 1.0
C B:MOH9001 3.3 43.6 1.0
CD B:GLU243 3.4 49.0 1.0
CG B:HIS246 3.4 41.1 1.0
OE2 B:GLU144 3.4 29.6 1.0
OE2 B:GLU243 3.6 51.0 1.0
CG B:GLU209 3.8 40.7 1.0
O B:HOH9197 3.8 35.9 1.0
CB B:HIS246 3.9 41.5 1.0
OE2 B:GLU209 3.9 39.6 1.0
NE2 B:GLN140 4.0 34.2 1.0
NE2 B:HIS246 4.2 40.6 1.0
ND1 B:HIS147 4.4 23.3 1.0
CD2 B:HIS246 4.4 40.3 1.0
CE1 B:HIS147 4.5 22.7 1.0
CD B:GLN140 4.7 36.2 1.0
OE1 B:GLU114 4.7 31.9 1.0
CG B:GLU144 4.7 27.2 1.0
CG B:GLU243 4.7 46.2 1.0
CG B:GLN140 4.8 34.4 1.0

Reference:

D.A.Whittington, M.H.Sazinsky, S.J.Lippard. X-Ray Crystal Structure of Alcohol Products Bound at the Active Site of Soluble Methane Monooxygenase Hydroxylase. J.Am.Chem.Soc. V. 123 1794 2001.
ISSN: ISSN 0002-7863
PubMed: 11456795
DOI: 10.1021/JA0031725
Page generated: Sat Aug 3 05:40:34 2024

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