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Iron in PDB 1fz7: Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol, PDB code: 1fz7 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) 30.00 / 1.96
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.400, 172.370, 221.130, 90.00, 90.00, 90.00
R / Rfree (%) 21.4 / 25.5

Other elements in 1fz7:

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol 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 III Soaked in 0.9 M Ethanol (pdb code 1fz7). 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 Soaked in 0.9 M Ethanol, PDB code: 1fz7:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz7

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Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


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 Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:42.6
occ:1.00
OE1 A:GLU114 2.1 42.0 1.0
ND1 A:HIS147 2.1 31.5 1.0
O2 A:FMT9001 2.4 51.1 1.0
OE2 A:GLU144 2.5 41.6 1.0
O A:HOH9128 2.5 44.9 1.0
CD A:GLU114 3.0 41.0 1.0
CE1 A:HIS147 3.0 33.5 1.0
FE A:FE5002 3.1 50.0 1.0
CG A:HIS147 3.2 31.1 1.0
OE2 A:GLU114 3.3 46.5 1.0
C A:FMT9001 3.3 53.1 1.0
CD A:GLU144 3.4 39.3 1.0
OE1 A:GLU144 3.5 38.6 1.0
CB A:HIS147 3.6 28.6 1.0
OE2 A:GLU243 4.0 63.6 1.0
O1 A:FMT9001 4.1 57.4 1.0
NE2 A:HIS147 4.2 35.1 1.0
CD2 A:HIS147 4.3 32.4 1.0
CG A:GLU114 4.4 38.8 1.0
CE1 A:HIS246 4.5 46.2 1.0
ND1 A:HIS246 4.5 49.7 1.0
OE2 A:GLU209 4.6 54.4 1.0
CG2 A:ILE239 4.6 34.8 1.0
CB A:GLU114 4.8 34.4 1.0
CG A:GLU144 4.8 34.7 1.0
OE1 A:GLU243 4.8 59.9 1.0
CD A:GLU243 4.8 61.8 1.0
CA A:GLU114 4.8 36.0 1.0
CA A:GLU144 4.9 29.0 1.0

Iron binding site 2 out of 4 in 1fz7

Go back to Iron Binding Sites List in 1fz7
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


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 Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:50.0
occ:1.00
OE2 A:GLU209 2.0 54.4 1.0
ND1 A:HIS246 2.3 49.7 1.0
O2 A:FMT9001 2.5 51.1 1.0
OE1 A:GLU144 2.6 38.6 1.0
OE1 A:GLU243 2.7 59.9 1.0
OE2 A:GLU243 2.9 63.6 1.0
CD A:GLU209 3.1 56.8 1.0
FE A:FE5001 3.1 42.6 1.0
CD A:GLU243 3.1 61.8 1.0
CE1 A:HIS246 3.1 46.2 1.0
CG A:HIS246 3.4 48.5 1.0
CD A:GLU144 3.5 39.3 1.0
C A:FMT9001 3.6 53.1 1.0
OE2 A:GLU144 3.7 41.6 1.0
NE2 A:GLN140 3.7 38.9 1.0
CB A:HIS246 3.8 49.5 1.0
OE1 A:GLU209 3.9 59.3 1.0
CG A:GLU209 4.0 56.4 1.0
O A:HOH9128 4.2 44.9 1.0
NE2 A:HIS246 4.3 48.2 1.0
ND1 A:HIS147 4.5 31.5 1.0
CD2 A:HIS246 4.5 47.1 1.0
CE1 A:HIS147 4.5 33.5 1.0
CD A:GLN140 4.5 40.8 1.0
O1 A:FMT9001 4.6 57.4 1.0
CG A:GLU243 4.6 58.8 1.0
CG A:GLN140 4.8 35.2 1.0
OE1 A:GLU114 4.9 42.0 1.0
CB A:GLU209 4.9 54.6 1.0
CG A:GLU144 4.9 34.7 1.0

Iron binding site 3 out of 4 in 1fz7

Go back to Iron Binding Sites List in 1fz7
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


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 Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:34.2
occ:1.00
OE1 B:GLU114 2.0 28.6 1.0
ND1 B:HIS147 2.1 27.1 1.0
O B:HOH9227 2.1 32.0 1.0
O B:EOH9002 2.2 46.0 1.0
OE2 B:GLU144 2.2 29.9 1.0
O B:HOH9103 2.4 33.4 1.0
CD B:GLU114 3.0 30.3 1.0
CE1 B:HIS147 3.0 25.2 1.0
CG B:HIS147 3.1 22.7 1.0
FE B:FE5004 3.2 44.6 1.0
CD B:GLU144 3.2 30.3 1.0
OE2 B:GLU114 3.4 34.1 1.0
OE1 B:GLU144 3.5 33.5 1.0
CB B:HIS147 3.5 25.8 1.0
C1 B:EOH9002 3.6 49.7 1.0
C2 B:EOH9002 4.1 47.7 1.0
NE2 B:HIS147 4.2 27.3 1.0
OE2 B:GLU243 4.2 58.7 1.0
CD2 B:HIS147 4.2 25.9 1.0
CE1 B:HIS246 4.3 43.6 1.0
CG B:GLU114 4.3 28.2 1.0
ND1 B:HIS246 4.4 43.0 1.0
CB B:GLU114 4.6 28.4 1.0
CA B:GLU144 4.6 28.0 1.0
CG B:GLU144 4.6 27.5 1.0
OE1 B:GLU243 4.7 51.7 1.0
CA B:GLU114 4.7 32.7 1.0
CG2 B:ILE239 4.7 31.4 1.0
OE1 B:GLU209 4.8 53.0 1.0
CD B:GLU243 4.9 56.1 1.0
CB B:GLU144 5.0 26.3 1.0

Iron binding site 4 out of 4 in 1fz7

Go back to Iron Binding Sites List in 1fz7
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked in 0.9 M Ethanol


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 Soaked in 0.9 M Ethanol within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:44.6
occ:1.00
O B:HOH9227 1.8 32.0 1.0
ND1 B:HIS246 2.1 43.0 1.0
OE1 B:GLU209 2.2 53.0 1.0
OE1 B:GLU144 2.3 33.5 1.0
OE1 B:GLU243 2.5 51.7 1.0
O B:EOH9002 2.6 46.0 1.0
CE1 B:HIS246 2.9 43.6 1.0
CD B:GLU209 2.9 55.6 1.0
FE B:FE5003 3.2 34.2 1.0
CG B:HIS246 3.2 44.7 1.0
CD B:GLU144 3.3 30.3 1.0
CD B:GLU243 3.5 56.1 1.0
OE2 B:GLU144 3.5 29.9 1.0
C1 B:EOH9002 3.6 49.7 1.0
CB B:HIS246 3.7 44.5 1.0
OE2 B:GLU243 3.7 58.7 1.0
OE2 B:GLU209 3.7 55.5 1.0
CG B:GLU209 3.7 54.0 1.0
NE2 B:GLN140 4.0 44.6 1.0
NE2 B:HIS246 4.1 47.7 1.0
CD2 B:HIS246 4.3 46.8 1.0
O B:HOH9103 4.4 33.4 1.0
ND1 B:HIS147 4.4 27.1 1.0
CD B:GLN140 4.5 43.0 1.0
CE1 B:HIS147 4.5 25.2 1.0
CG B:GLN140 4.6 39.1 1.0
CG B:GLU144 4.7 27.5 1.0
CG B:GLU243 4.8 50.9 1.0
OE1 B:GLU114 4.8 28.6 1.0
C2 B:EOH9002 4.9 47.7 1.0
CB B:GLU209 4.9 51.7 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 05:40:33 2024

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