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Iron in PDB 1fz5: Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme, PDB code: 1fz5 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) 46.40 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.240, 171.570, 220.520, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 25.3

Other elements in 1fz5:

The structure of Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme (pdb code 1fz5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme, PDB code: 1fz5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1fz5

Go back to Iron Binding Sites List in 1fz5
Iron binding site 1 out of 2 in the Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme


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 Crystallized Anaerobically From Reduced Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:57.0
occ:1.00
OE2 A:GLU144 2.2 50.9 1.0
ND1 A:HIS147 2.3 38.4 1.0
OE1 A:GLU114 2.5 56.9 1.0
OE2 A:GLU114 2.6 54.9 1.0
CD A:GLU114 2.8 53.8 1.0
CE1 A:HIS147 3.2 39.4 1.0
CE1 A:HIS246 3.2 66.8 1.0
CD A:GLU144 3.4 48.5 1.0
CG A:HIS147 3.4 36.8 1.0
OE2 A:GLU209 3.7 65.7 1.0
ND1 A:HIS246 3.8 66.4 1.0
CB A:HIS147 3.8 33.8 1.0
OE1 A:GLU144 4.1 49.9 1.0
O A:HOH5138 4.2 62.1 1.0
CG A:GLU114 4.2 50.0 1.0
NE2 A:HIS147 4.4 38.7 1.0
NE2 A:HIS246 4.4 66.9 1.0
CG A:GLU144 4.5 45.7 1.0
CD2 A:HIS147 4.5 38.5 1.0
CG2 A:ILE239 4.6 40.3 1.0
CB A:GLU114 4.7 45.4 1.0
CA A:GLU114 4.9 42.2 1.0
CD A:GLU209 5.0 67.4 1.0
CA A:GLU144 5.0 37.9 1.0

Iron binding site 2 out of 2 in 1fz5

Go back to Iron Binding Sites List in 1fz5
Iron binding site 2 out of 2 in the Methane Monooxygenase Hydroxylase, Form II Crystallized Anaerobically From Reduced Enzyme


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 Crystallized Anaerobically From Reduced Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:58.8
occ:0.99
OE1 B:GLU114 2.2 41.5 1.0
ND1 B:HIS147 2.2 33.1 1.0
OE2 B:GLU144 2.4 44.1 1.0
CD B:GLU114 3.0 41.8 1.0
CE1 B:HIS147 3.1 33.2 1.0
OE2 B:GLU114 3.1 44.7 1.0
CE1 B:HIS246 3.2 69.6 1.0
CG B:HIS147 3.3 32.8 1.0
CD B:GLU144 3.4 42.4 1.0
OE1 B:GLU144 3.6 45.2 1.0
OE1 B:GLU243 3.7 67.9 1.0
CB B:HIS147 3.7 32.1 1.0
ND1 B:HIS246 3.7 69.1 1.0
OE1 B:GLU209 3.9 72.0 1.0
NE2 B:HIS147 4.3 32.2 1.0
NE2 B:HIS246 4.3 69.7 1.0
CD2 B:HIS147 4.4 30.1 1.0
CG B:GLU114 4.4 42.3 1.0
CD B:GLU243 4.5 67.4 1.0
CA B:GLU144 4.7 39.3 1.0
OE2 B:GLU243 4.7 68.7 1.0
CG2 B:ILE239 4.7 36.8 1.0
CG B:GLU144 4.7 41.6 1.0
CB B:GLU114 4.9 41.7 1.0
CA B:GLU114 5.0 40.6 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 05:40:33 2024

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