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Iron in PDB 1fz0: Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically, PDB code: 1fz0 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) 30.00 / 2.07
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.420, 171.710, 221.490, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 23

Other elements in 1fz0:

The structure of Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically 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 Mixed-Valent Grown Anaerobically (pdb code 1fz0). 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 Grown Anaerobically, PDB code: 1fz0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz0

Go back to Iron Binding Sites List in 1fz0
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:30.7
occ:1.00
 O A:HOH5310 1.6 53.8 1.0
OE1 A:GLU114 2.0 32.7 1.0
ND1 A:HIS147 2.2 20.5 1.0
OE2 A:GLU144 2.2 27.3 1.0
O A:HOH5151 2.5 40.7 1.0
O A:HOH5152 2.5 29.9 1.0
CD A:GLU114 3.1 32.9 1.0
CE1 A:HIS147 3.1 24.0 1.0
CD A:GLU144 3.1 28.9 1.0
CG A:HIS147 3.3 20.0 1.0
OE1 A:GLU144 3.3 28.4 1.0
FE A:FE25002 3.4 49.0 1.0
OE2 A:GLU114 3.4 36.8 1.0
CB A:HIS147 3.6 20.5 1.0
OE2 A:GLU243 3.9 50.5 1.0
CE1 A:HIS246 4.1 37.1 1.0
NE2 A:HIS147 4.2 23.5 1.0
CD2 A:HIS147 4.3 24.3 1.0
ND1 A:HIS246 4.4 40.1 1.0
CG A:GLU114 4.4 29.6 1.0
O A:HOH5300 4.4 47.5 1.0
OE2 A:GLU209 4.5 52.9 1.0
CG A:GLU144 4.6 24.4 1.0
CA A:GLU144 4.7 19.2 1.0
CB A:GLU114 4.7 21.7 1.0
CA A:GLU114 4.7 23.3 1.0
CD A:GLU243 4.9 50.3 1.0
CG2 A:ILE239 4.9 22.9 1.0

Iron binding site 2 out of 4 in 1fz0

Go back to Iron Binding Sites List in 1fz0
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:49.0
occ:1.00
 O A:HOH5310 1.8 53.8 1.0
ND1 A:HIS246 2.0 40.1 1.0
OE2 A:GLU209 2.1 52.9 1.0
OE1 A:GLU243 2.3 51.1 1.0
OE2 A:GLU243 2.8 50.5 1.0
CD A:GLU243 2.9 50.3 1.0
CE1 A:HIS246 2.9 37.1 1.0
O A:HOH5152 3.1 29.9 1.0
CG A:HIS246 3.1 37.0 1.0
CD A:GLU209 3.2 48.3 1.0
OE1 A:GLU144 3.4 28.4 1.0
FE A:FE25001 3.4 30.7 1.0
CB A:HIS246 3.5 34.2 1.0
O A:HOH5151 3.8 40.7 1.0
OE1 A:GLU209 4.0 52.0 1.0
CG A:GLU209 4.0 46.7 1.0
NE2 A:HIS246 4.1 38.0 1.0
CD2 A:HIS246 4.2 36.5 1.0
NE2 A:GLN140 4.2 27.9 1.0
CD A:GLU144 4.3 28.9 1.0
CG A:GLU243 4.4 45.7 1.0
OE2 A:GLU144 4.4 27.3 1.0
CE1 A:HIS147 4.5 24.0 1.0
ND1 A:HIS147 4.6 20.5 1.0
CB A:GLU209 4.8 37.5 1.0
CD A:GLN140 4.9 27.4 1.0
CA A:GLU243 5.0 39.4 1.0
OD1 A:ASN214 5.0 55.7 1.0

Iron binding site 3 out of 4 in 1fz0

Go back to Iron Binding Sites List in 1fz0
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:30.0
occ:1.00
 O B:HOH5284 1.7 49.8 1.0
OE1 B:GLU114 1.9 28.9 1.0
ND1 B:HIS147 2.2 23.5 1.0
OE2 B:GLU144 2.3 30.1 1.0
O B:HOH5129 2.4 33.3 1.0
O B:HOH5130 2.6 34.4 1.0
CD B:GLU114 2.8 28.0 1.0
OE2 B:GLU114 3.1 36.4 1.0
CE1 B:HIS147 3.1 27.8 1.0
CD B:GLU144 3.2 27.8 1.0
CG B:HIS147 3.3 22.9 1.0
OE1 B:GLU144 3.4 28.2 1.0
FE B:FE25004 3.4 53.0 1.0
CB B:HIS147 3.6 21.7 1.0
OE2 B:GLU243 3.9 49.6 1.0
CG B:GLU114 4.2 25.6 1.0
NE2 B:HIS147 4.3 28.5 1.0
CE1 B:HIS246 4.3 38.6 1.0
CD2 B:HIS147 4.4 21.1 1.0
OE2 B:GLU209 4.4 53.9 1.0
ND1 B:HIS246 4.5 37.1 1.0
CA B:GLU144 4.6 23.0 1.0
CG B:GLU144 4.6 26.8 1.0
CB B:GLU114 4.6 21.9 1.0
CA B:GLU114 4.7 22.7 1.0
CG2 B:ILE239 4.8 23.3 1.0
CD B:GLU243 5.0 48.4 1.0

Iron binding site 4 out of 4 in 1fz0

Go back to Iron Binding Sites List in 1fz0
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Mixed-Valent Grown Anaerobically


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 Grown Anaerobically within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:53.0
occ:1.00
 O B:HOH5284 1.8 49.8 1.0
OE2 B:GLU209 1.9 53.9 1.0
ND1 B:HIS246 2.2 37.1 1.0
OE1 B:GLU243 2.3 49.4 1.0
OE2 B:GLU243 2.5 49.6 1.0
CD B:GLU243 2.8 48.4 1.0
CD B:GLU209 3.1 49.3 1.0
CE1 B:HIS246 3.1 38.6 1.0
O B:HOH5130 3.2 34.4 1.0
CG B:HIS246 3.3 38.8 1.0
FE B:FE25003 3.4 30.0 1.0
O B:HOH5129 3.6 33.3 1.0
OE1 B:GLU144 3.6 28.2 1.0
CB B:HIS246 3.7 35.7 1.0
CG B:GLU209 3.9 46.3 1.0
OE1 B:GLU209 3.9 48.1 1.0
NE2 B:HIS246 4.3 38.6 1.0
CG B:GLU243 4.3 44.2 1.0
CD2 B:HIS246 4.4 38.5 1.0
CE1 B:HIS147 4.4 27.8 1.0
CD B:GLU144 4.4 27.8 1.0
NE2 B:GLN140 4.5 31.2 1.0
OE2 B:GLU144 4.5 30.1 1.0
ND1 B:HIS147 4.5 23.5 1.0
CB B:GLU209 4.7 39.8 1.0
OD1 B:ASN214 4.8 53.4 1.0
CA B:GLU243 4.9 37.7 1.0
CD B:GLN140 5.0 33.6 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 05:32:16 2024

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