Iron in PDB 3rnc: Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase T201S/I100A Double Mutant

The structure of Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase T201S/I100A Double Mutant, PDB code: 3rnc was solved by G.Gucinski, W.J.Song, S.J.Lippard, M.H.Sazinsky, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.64 / 2.74
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	182.571, 182.571, 67.047, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 26.5

The binding sites of Iron atom in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase T201S/I100A Double Mutant (pdb code 3rnc). 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 T201S/I100A Double Mutant, PDB code: 3rnc:
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 T201S/I100A Double Mutant


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 T201S/I100A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe499 b:68.5 occ:1.00 OE2 A:GLU197 1.8 63.6 1.0 O A:OH501 1.8 52.2 1.0 OE2 A:GLU134 2.1 54.8 1.0 O1 A:EDO502 2.2 66.8 1.0 OE2 A:GLU231 2.3 65.0 1.0 NE2 A:HIS234 2.4 57.0 1.0 CD A:GLU197 3.0 62.8 1.0 FE A:FE500 3.0 58.6 1.0 C1 A:EDO502 3.0 66.8 1.0 CD A:GLU231 3.1 67.7 1.0 CD A:GLU134 3.2 55.3 1.0 CE1 A:HIS234 3.2 58.5 1.0 O A:HOH503 3.3 56.4 1.0 OE1 A:GLU231 3.3 71.3 1.0 O A:HOH504 3.3 47.7 1.0 CD2 A:HIS234 3.4 54.2 1.0 OE1 A:GLU134 3.6 51.0 1.0 CG A:GLU197 3.7 62.6 1.0 OE1 A:GLU197 3.9 63.8 1.0 ND1 A:HIS234 4.4 57.6 1.0 CG A:GLU231 4.4 64.8 1.0 CG A:GLU134 4.5 54.6 1.0 C2 A:EDO502 4.5 67.2 1.0 ND1 A:HIS137 4.5 55.5 1.0 CG A:HIS234 4.5 55.2 1.0 CB A:GLU197 4.6 63.9 1.0 CE1 A:HIS137 4.6 56.2 1.0 OE1 A:GLU104 4.8 54.0 1.0

Iron binding site 2 out of 2 in the Structure of the Toluene/O-Xylene Monooxygenase Hydroxylase T201S/I100A Double Mutant


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 T201S/I100A Double Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe500 b:58.6 occ:1.00 O A:HOH504 1.8 47.7 1.0 OE1 A:GLU134 1.9 51.0 1.0 OE1 A:GLU104 2.0 54.0 1.0 ND1 A:HIS137 2.0 55.5 1.0 O A:OH501 2.3 52.2 1.0 O1 A:EDO502 2.5 66.8 1.0 CD A:GLU134 2.7 55.3 1.0 CE1 A:HIS137 2.8 56.2 1.0 OE2 A:GLU134 2.9 54.8 1.0 FE A:FE499 3.0 68.5 1.0 CD A:GLU104 3.1 51.1 1.0 CG A:HIS137 3.2 55.9 1.0 CB A:HIS137 3.7 55.3 1.0 OE2 A:GLU104 3.7 47.2 1.0 C1 A:EDO502 3.9 66.8 1.0 OE1 A:GLU231 4.0 71.3 1.0 NE2 A:HIS137 4.0 55.9 1.0 CG A:GLU134 4.1 54.6 1.0 CD2 A:HIS137 4.2 55.1 1.0 CG A:GLU104 4.3 48.7 1.0 OE2 A:GLU231 4.4 65.0 1.0 NE2 A:HIS234 4.6 57.0 1.0 CB A:GLU104 4.6 46.8 1.0 CA A:GLU134 4.6 53.9 1.0 CD A:GLU231 4.6 67.7 1.0 OE2 A:GLU197 4.7 63.6 1.0 CE1 A:HIS234 4.7 58.5 1.0 C2 A:EDO502 4.7 67.2 1.0 CB A:GLU134 4.7 53.2 1.0 CG2 A:ILE227 4.7 58.9 1.0 O2 A:EDO502 4.9 67.1 1.0

W.J.Song, G.Gucinski, M.H.Sazinsky, S.J.Lippard. Tracking A Defined Route For O2 Migration in A Dioxygen-Activating Diiron Enzyme. Proc.Natl.Acad.Sci.Usa V. 108 14795 2011.
ISSN: ISSN 0027-8424
PubMed: 21859951
DOI: 10.1073/PNAS.1106514108