Iron in PDB 3i63: Peroxide Bound Toluene 4-Monooxygenase

The structure of Peroxide Bound Toluene 4-Monooxygenase, PDB code: 3i63 was solved by L.J.Bailey, B.G.Fox, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.40 / 2.09
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	98.792, 116.929, 181.608, 90.00, 90.00, 90.00
R / Rfree (%)	15.6 / 20.1

The binding sites of Iron atom in the Peroxide Bound Toluene 4-Monooxygenase (pdb code 3i63). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Peroxide Bound Toluene 4-Monooxygenase, PDB code: 3i63:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Peroxide Bound Toluene 4-Monooxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Peroxide Bound Toluene 4-Monooxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:21.0 occ:1.00 O A:HOH504 1.9 11.0 1.0 OE1 A:GLU231 2.0 15.3 1.0 OE2 A:GLU197 2.1 20.3 1.0 OE1 A:GLU134 2.1 12.2 1.0 NE2 A:HIS234 2.2 13.3 1.0 O2 A:PEO6079 2.4 21.7 0.7 CD A:GLU197 3.0 18.1 1.0 CD A:GLU231 3.1 19.2 1.0 CD A:GLU134 3.1 14.0 1.0 CE1 A:HIS234 3.1 9.2 1.0 O1 A:PEO6079 3.2 15.3 0.7 CD2 A:HIS234 3.2 11.9 1.0 FE A:FE502 3.3 20.6 1.0 OE2 A:GLU134 3.5 12.7 1.0 OE2 A:GLU231 3.6 16.5 1.0 O A:HOH512 3.6 16.8 1.0 CG A:GLU197 3.7 12.9 1.0 OE1 A:GLU197 3.9 26.8 1.0 ND1 A:HIS234 4.3 11.4 1.0 CG A:HIS234 4.3 12.4 1.0 CG A:GLU231 4.4 13.6 1.0 O A:HOH508 4.4 15.0 1.0 O A:HOH513 4.4 18.2 1.0 CG A:GLU134 4.4 9.7 1.0 CB A:GLU231 4.4 11.1 1.0 CA A:GLU231 4.6 13.0 1.0 CB A:GLU197 4.7 13.9 1.0 ND1 A:HIS137 4.8 11.8 1.0 CE1 A:HIS137 4.8 9.1 1.0

Iron binding site 2 out of 2 in the Peroxide Bound Toluene 4-Monooxygenase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Peroxide Bound Toluene 4-Monooxygenase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe502 b:20.6 occ:1.00 OE2 A:GLU134 2.0 12.7 1.0 O A:HOH508 2.0 15.0 1.0 O A:HOH504 2.1 11.0 1.0 O1 A:PEO6079 2.2 15.3 0.7 OE2 A:GLU104 2.2 11.6 1.0 ND1 A:HIS137 2.3 11.8 1.0 CD A:GLU134 3.0 14.0 1.0 CD A:GLU104 3.2 11.8 1.0 O2 A:PEO6079 3.2 21.7 0.7 CE1 A:HIS137 3.2 9.1 1.0 OE1 A:GLU134 3.3 12.2 1.0 FE A:FE501 3.3 21.0 1.0 CG A:HIS137 3.4 9.1 1.0 OE1 A:GLU104 3.5 14.2 1.0 CB A:HIS137 3.7 11.1 1.0 O A:HOH513 4.1 18.2 1.0 NE2 A:HIS137 4.4 9.6 1.0 CG A:GLU134 4.4 9.7 1.0 CD2 A:HIS137 4.5 9.3 1.0 CG A:GLU104 4.5 12.7 1.0 OE1 A:GLU231 4.6 15.3 1.0 CG2 A:ILE227 4.6 9.8 1.0 NE2 A:HIS234 4.6 13.3 1.0 CE1 A:HIS234 4.7 9.2 1.0 CA A:GLU134 4.7 10.6 1.0 CB A:GLU104 4.7 11.4 1.0 O1 A:PEO503 4.8 48.6 1.0 CB A:GLU134 4.9 11.2 1.0

L.J.Bailey, B.G.Fox. Crystallographic and Catalytic Studies of the Peroxide-Shunt Reaction in A Diiron Hydroxylase. Biochemistry V. 48 8932 2009.
ISSN: ISSN 0006-2960
PubMed: 19705873
DOI: 10.1021/BI901150A