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Iron in PDB 1fz2: Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking, PDB code: 1fz2 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) 29.83 / 2.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.370, 171.886, 221.509, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 22.9

Other elements in 1fz2:

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking (pdb code 1fz2). 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 Mixed-Valent Generated By Crystal Soaking, PDB code: 1fz2:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz2

Go back to Iron Binding Sites List in 1fz2
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking


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 Mixed-Valent Generated By Crystal Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:37.9
occ:1.00
 O A:HOH5277 1.7 66.2 1.0
OE1 A:GLU114 2.0 40.6 1.0
ND1 A:HIS147 2.2 25.4 1.0
OE2 A:GLU144 2.2 31.4 1.0
O A:HOH5167 2.6 36.7 1.0
O A:HOH5168 2.7 45.8 1.0
CD A:GLU114 3.0 39.1 1.0
CE1 A:HIS147 3.1 27.3 1.0
CD A:GLU144 3.2 31.8 1.0
CG A:HIS147 3.2 23.8 1.0
OE2 A:GLU114 3.3 42.2 1.0
FE A:FE25002 3.4 63.1 1.0
OE1 A:GLU144 3.4 29.7 1.0
CB A:HIS147 3.5 22.7 1.0
OE2 A:GLU243 3.8 55.0 1.0
CE1 A:HIS246 4.2 43.4 1.0
NE2 A:HIS147 4.2 30.5 1.0
CG A:GLU114 4.3 32.1 1.0
CD2 A:HIS147 4.3 27.4 1.0
ND1 A:HIS246 4.4 46.5 1.0
OE2 A:GLU209 4.5 53.6 1.0
CG A:GLU144 4.6 24.9 1.0
CB A:GLU114 4.6 25.7 1.0
CA A:GLU144 4.6 22.0 1.0
CA A:GLU114 4.7 27.7 1.0
CD A:GLU243 4.8 56.1 1.0
CG2 A:ILE239 4.8 26.7 1.0
CB A:GLU144 4.9 21.9 1.0

Iron binding site 2 out of 4 in 1fz2

Go back to Iron Binding Sites List in 1fz2
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking


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 Mixed-Valent Generated By Crystal Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:63.1
occ:1.00
 O A:HOH5277 1.8 66.2 1.0
ND1 A:HIS246 2.1 46.5 1.0
OE2 A:GLU209 2.2 53.6 1.0
OE1 A:GLU243 2.4 54.2 1.0
OE2 A:GLU243 2.4 55.0 1.0
CD A:GLU243 2.7 56.1 1.0
CE1 A:HIS246 3.0 43.4 1.0
CG A:HIS246 3.2 44.3 1.0
CD A:GLU209 3.2 48.8 1.0
O A:HOH5167 3.2 36.7 1.0
OE1 A:GLU144 3.4 29.7 1.0
FE A:FE25001 3.4 37.9 1.0
CB A:HIS246 3.6 42.8 1.0
OE1 A:GLU209 3.9 50.2 1.0
O A:HOH5168 3.9 45.8 1.0
CG A:GLU209 4.0 48.7 1.0
NE2 A:GLN140 4.1 30.4 1.0
NE2 A:HIS246 4.1 42.5 1.0
CD2 A:HIS246 4.2 42.9 1.0
CG A:GLU243 4.2 51.3 1.0
CD A:GLU144 4.2 31.8 1.0
OE2 A:GLU144 4.3 31.4 1.0
CE1 A:HIS147 4.4 27.3 1.0
ND1 A:HIS147 4.5 25.4 1.0
CB A:GLU209 4.8 40.8 1.0
CA A:GLU243 4.8 44.1 1.0
CD A:GLN140 4.9 33.5 1.0
CB A:GLU243 4.9 46.2 1.0

Iron binding site 3 out of 4 in 1fz2

Go back to Iron Binding Sites List in 1fz2
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking


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 Mixed-Valent Generated By Crystal Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:34.2
occ:1.00
 OE1 B:GLU114 2.0 32.6 1.0
ND1 B:HIS147 2.2 25.5 1.0
OE2 B:GLU144 2.2 31.9 1.0
O B:HOH5255 2.5 31.1 1.0
O B:HOH5143 2.6 42.4 1.0
O B:HOH5094 2.8 39.8 1.0
CD B:GLU114 3.0 31.5 1.0
CE1 B:HIS147 3.1 25.7 1.0
CD B:GLU144 3.1 31.9 1.0
CG B:HIS147 3.3 22.4 1.0
OE1 B:GLU144 3.3 32.2 1.0
OE2 B:GLU114 3.4 40.9 1.0
FE B:FE25004 3.4 66.6 1.0
CB B:HIS147 3.7 21.8 1.0
OE2 B:GLU243 3.7 62.6 1.0
CE1 B:HIS246 4.0 46.0 1.0
ND1 B:HIS246 4.2 45.4 1.0
NE2 B:HIS147 4.2 30.0 1.0
CD2 B:HIS147 4.3 24.4 1.0
CG B:GLU114 4.4 28.8 1.0
CG B:GLU144 4.6 29.8 1.0
CA B:GLU144 4.6 26.8 1.0
OE1 B:GLU209 4.7 55.3 1.0
CB B:GLU114 4.7 25.8 1.0
CG2 B:ILE239 4.8 25.1 1.0
CD B:GLU243 4.8 60.9 1.0
CA B:GLU114 4.8 27.3 1.0
CB B:GLU144 5.0 28.5 1.0

Iron binding site 4 out of 4 in 1fz2

Go back to Iron Binding Sites List in 1fz2
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Generated By Crystal Soaking


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 Mixed-Valent Generated By Crystal Soaking within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:66.6
occ:1.00
 O B:HOH5255 1.5 31.1 1.0
ND1 B:HIS246 2.0 45.4 1.0
OE2 B:GLU243 2.5 62.6 1.0
OE1 B:GLU243 2.5 65.0 1.0
CD B:GLU243 2.8 60.9 1.0
OE1 B:GLU209 2.8 55.3 1.0
CE1 B:HIS246 2.9 46.0 1.0
CG B:HIS246 3.0 45.2 1.0
CD B:GLU209 3.2 54.5 1.0
CB B:HIS246 3.4 42.3 1.0
FE B:FE25003 3.4 34.2 1.0
OE1 B:GLU144 3.6 32.2 1.0
O B:HOH5094 3.7 39.8 1.0
O B:HOH5143 3.8 42.4 1.0
CG B:GLU209 3.8 49.4 1.0
OE2 B:GLU209 3.8 54.1 1.0
NE2 B:HIS246 4.0 45.9 1.0
CD2 B:HIS246 4.1 44.9 1.0
CG B:GLU243 4.2 55.5 1.0
CD B:GLU144 4.4 31.9 1.0
CA B:GLU243 4.5 42.5 1.0
CE1 B:HIS147 4.5 25.7 1.0
NE2 B:GLN140 4.5 34.1 1.0
OE2 B:GLU144 4.5 31.9 1.0
ND1 B:HIS147 4.6 25.5 1.0
CB B:GLU209 4.8 44.6 1.0
CB B:GLU243 4.8 46.1 1.0
CA B:HIS246 4.9 43.9 1.0
CD B:GLN140 5.0 33.2 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: Sun Dec 13 14:14:46 2020

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