Iron in PDB 1mhz: Methane Monooxygenase Hydroxylase

All present enzymatic activity of Methane Monooxygenase Hydroxylase:
1.14.13.25;

The structure of Methane Monooxygenase Hydroxylase, PDB code: 1mhz was solved by N.Elango, R.Radhakrishnan, W.A.Froland, B.J.Waller, C.A.Earhart, J.D.Lipscomb, D.H.Ohlendorf, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	293.380, 64.010, 143.650, 90.00, 90.00, 90.00
R / Rfree (%)	15.2 / n/a

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase (pdb code 1mhz). 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, PDB code: 1mhz:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Methane Monooxygenase Hydroxylase


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 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:22.0 occ:1.00 H1 D:HOH803 1.3 0.0 1.0 H2 D:HOH803 1.7 0.0 1.0 O D:HOH803 1.8 39.8 1.0 H2 D:HOH805 1.8 0.0 1.0 HD1 D:HIS147 1.8 0.0 1.0 O D:HOH804 1.9 25.2 1.0 OE1 D:GLU114 2.0 23.7 1.0 OE1 D:GLU144 2.3 19.2 1.0 O D:HOH805 2.4 9.2 1.0 H2 D:HOH804 2.5 0.0 1.0 H1 D:HOH804 2.5 0.0 1.0 ND1 D:HIS147 2.6 22.0 1.0 H1 D:HOH805 3.0 0.0 1.0 FE D:FE802 3.1 23.5 1.0 CD D:GLU114 3.1 25.2 1.0 H1 D:HOH806 3.3 0.0 1.0 CD D:GLU144 3.3 17.6 1.0 CG D:HIS147 3.4 20.7 1.0 CB D:HIS147 3.6 14.4 1.0 CE1 D:HIS147 3.6 21.6 1.0 OE2 D:GLU144 3.6 21.3 1.0 OE2 D:GLU114 3.6 28.2 1.0 OE2 D:GLU243 3.8 42.2 1.0 HD1 D:HIS246 4.1 0.0 1.0 O D:HOH806 4.2 31.5 1.0 OE1 D:GLU243 4.3 48.3 1.0 CG D:GLU114 4.3 23.4 1.0 CD D:GLU243 4.4 42.4 1.0 CE1 D:HIS246 4.4 20.6 1.0 CB D:GLU114 4.5 21.4 1.0 CA D:GLU114 4.6 20.9 1.0 CD2 D:HIS147 4.6 19.5 1.0 NE2 D:HIS147 4.6 23.2 1.0 ND1 D:HIS246 4.6 21.3 1.0 CA D:GLU144 4.6 13.4 1.0 H2 D:HOH806 4.7 0.0 1.0 CG D:GLU144 4.7 19.3 1.0 O D:ASP143 4.8 14.9 1.0 CG1 D:VAL239 5.0 17.7 1.0 CB D:GLU144 5.0 15.4 1.0

Iron binding site 2 out of 2 in the Methane Monooxygenase Hydroxylase


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 within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe802 b:23.5 occ:1.00 HD1 D:HIS246 1.3 0.0 1.0 H1 D:HOH803 1.9 0.0 1.0 OE2 D:GLU243 2.0 42.2 1.0 O D:HOH803 2.2 39.8 1.0 ND1 D:HIS246 2.3 21.3 1.0 OE2 D:GLU209 2.3 18.4 1.0 H2 D:HOH804 2.3 0.0 1.0 O D:HOH804 2.4 25.2 1.0 H2 D:HOH803 2.6 0.0 1.0 OE2 D:GLU144 2.6 21.3 1.0 CE1 D:HIS246 3.0 20.6 1.0 FE D:FE801 3.1 22.0 1.0 CD D:GLU243 3.2 42.4 1.0 CD D:GLU209 3.3 16.6 1.0 H1 D:HOH804 3.3 0.0 1.0 H2 D:HOH805 3.4 0.0 1.0 CD D:GLU144 3.4 17.6 1.0 CG D:HIS246 3.5 18.9 1.0 HE22 D:GLN140 3.5 0.0 1.0 OE1 D:GLU144 3.5 19.2 1.0 H1 D:HOH806 3.7 0.0 1.0 CG D:GLU209 3.7 15.6 1.0 H1 D:HOH805 3.8 0.0 1.0 NE2 D:GLN140 3.9 11.9 1.0 OE1 D:GLU243 3.9 48.3 1.0 CB D:HIS246 4.0 19.4 1.0 O D:HOH805 4.0 9.2 1.0 HE21 D:GLN140 4.1 0.0 1.0 HD1 D:HIS147 4.1 0.0 1.0 NE2 D:HIS246 4.2 21.4 1.0 CG D:GLU243 4.2 39.3 1.0 OE1 D:GLU209 4.3 16.2 1.0 CD2 D:HIS246 4.4 20.6 1.0 O D:HOH806 4.5 31.5 1.0 CB D:GLU209 4.6 19.3 1.0 H2 D:HOH806 4.6 0.0 1.0 CD D:GLN140 4.8 16.9 1.0 ND1 D:HIS147 4.8 22.0 1.0 CG D:GLU144 4.9 19.3 1.0 OE1 D:GLU114 4.9 23.7 1.0 CA D:GLU243 4.9 31.9 1.0 CB D:GLU243 5.0 31.9 1.0

N.Elango, R.Radhakrishnan, W.A.Froland, B.J.Wallar, C.A.Earhart, J.D.Lipscomb, D.H.Ohlendorf. Crystal Structure of the Hydroxylase Component of Methane Monooxygenase From Methylosinus Trichosporium OB3B Protein Sci. V. 6 556 1997.
ISSN: ISSN 0961-8368
PubMed: 9070438