Iron in PDB 1t0q: Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase

The structure of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase, PDB code: 1t0q was solved by M.H.Sazinsky, J.Bard, A.Di Donato, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.92 / 2.15
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.805, 182.805, 68.036, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 22.5

The binding sites of Iron atom in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase (pdb code 1t0q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase, PDB code: 1t0q:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe499 b:34.9 occ:1.00 OE2 A:GLU197 1.9 34.5 1.0 O A:OH501 2.0 26.9 1.0 O1 A:MCR502 2.1 55.9 1.0 OE2 A:GLU134 2.2 33.3 1.0 NE2 A:HIS234 2.2 31.6 1.0 OE1 A:GLU231 2.3 45.9 1.0 C1 A:MCR502 3.0 58.5 1.0 CD A:GLU134 3.0 27.4 1.0 CD A:GLU197 3.0 35.5 1.0 CE1 A:HIS234 3.1 30.0 1.0 FE A:FE500 3.1 29.1 1.0 OE1 A:GLU134 3.2 24.6 1.0 CD A:GLU231 3.2 49.5 1.0 CD2 A:HIS234 3.3 28.4 1.0 OE2 A:GLU231 3.5 51.9 1.0 O2 A:MCR502 3.6 62.0 1.0 O A:HOH505 3.7 31.8 1.0 CG A:GLU197 3.8 35.3 1.0 OE1 A:GLU197 3.9 35.0 1.0 C2 A:MCR502 3.9 56.6 1.0 O A:HOH580 4.1 28.1 1.0 ND1 A:HIS234 4.2 30.7 1.0 CG A:HIS234 4.4 30.6 1.0 CG A:GLU134 4.4 26.1 1.0 CG A:GLU231 4.5 47.0 1.0 ND1 A:HIS137 4.6 28.7 1.0 CE1 A:HIS137 4.7 30.1 1.0 OE1 A:GLU104 4.8 31.3 1.0 CB A:GLU197 4.8 34.3 1.0

Iron binding site 2 out of 2 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:29.1 occ:1.00 O A:HOH580 2.0 28.1 1.0 OE1 A:GLU134 2.1 24.6 1.0 ND1 A:HIS137 2.1 28.7 1.0 OE1 A:GLU104 2.2 31.3 1.0 O A:OH501 2.2 26.9 1.0 O1 A:MCR502 2.2 55.9 1.0 CE1 A:HIS137 2.9 30.1 1.0 CD A:GLU104 3.1 30.0 1.0 CD A:GLU134 3.1 27.4 1.0 FE A:FE499 3.1 34.9 1.0 CG A:HIS137 3.2 27.7 1.0 C1 A:MCR502 3.2 58.5 1.0 OE2 A:GLU104 3.4 27.0 1.0 OE2 A:GLU134 3.5 33.3 1.0 CB A:HIS137 3.6 26.1 1.0 O2 A:MCR502 3.7 62.0 1.0 OE2 A:GLU231 3.9 51.9 1.0 NE2 A:HIS137 4.1 27.9 1.0 CD2 A:HIS137 4.2 27.7 1.0 C2 A:MCR502 4.3 56.6 1.0 OE1 A:GLU231 4.4 45.9 1.0 CG A:GLU134 4.5 26.1 1.0 CG A:GLU104 4.5 28.7 1.0 CD A:GLU231 4.6 49.5 1.0 NE2 A:HIS234 4.6 31.6 1.0 CE1 A:HIS234 4.6 30.0 1.0 CG2 A:ILE227 4.6 38.1 1.0 CA A:GLU134 4.6 25.3 1.0 OE2 A:GLU197 4.8 34.5 1.0 CB A:GLU104 4.8 28.6 1.0 CB A:GLU134 4.9 24.3 1.0

M.H.Sazinsky, J.Bard, A.Di Donato, S.J.Lippard. Crystal Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase From Pseudomonas Stutzeri OX1: Insight Into the Substrate Specificity, Substrate Channeling, and Active Site Tuning of Multicomponent Monooxygenases. J.Biol.Chem. V. 279 30600 2004.
ISSN: ISSN 0021-9258
PubMed: 15096510
DOI: 10.1074/JBC.M400710200