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Iron in PDB 1xvd: Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure

Enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure

All present enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure:
1.14.13.25;

Protein crystallography data

The structure of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure, PDB code: 1xvd was solved by M.H.Sazinsky, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.94 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.182, 171.497, 221.304, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 22.9

Other elements in 1xvd:

The structure of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure also contains other interesting chemical elements:

Fluorine (F) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure (pdb code 1xvd). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure, PDB code: 1xvd:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1xvd

Go back to Iron Binding Sites List in 1xvd
Iron binding site 1 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe528

b:63.1
occ:1.00
 OE1 A:GLU114 2.1 61.1 1.0
ND1 A:HIS147 2.3 34.7 1.0
OE2 A:GLU144 2.7 42.3 1.0
FE A:FE529 2.8 78.5 1.0
CD A:GLU114 2.9 58.6 1.0
O A:HOH2862 2.9 52.4 1.0
OE2 A:GLU114 2.9 61.7 1.0
CE1 A:HIS147 3.0 34.7 1.0
O A:HOH2861 3.2 47.1 1.0
OE1 A:GLU144 3.4 44.0 1.0
CD A:GLU144 3.4 40.9 1.0
CG A:HIS147 3.5 32.8 1.0
CE1 A:HIS246 3.9 66.9 1.0
OE2 A:GLU243 3.9 62.8 1.0
ND1 A:HIS246 4.0 66.8 1.0
CB A:HIS147 4.0 31.0 1.0
NE2 A:HIS147 4.2 33.6 1.0
CG A:GLU114 4.4 53.3 1.0
CD2 A:HIS147 4.5 34.5 1.0
OE1 A:GLU243 4.5 64.5 1.0
CD A:GLU243 4.6 63.7 1.0
CG2 A:ILE239 4.7 38.7 1.0
OE2 A:GLU209 4.7 71.2 1.0
CB A:GLU114 4.9 45.8 1.0
CG A:GLU144 4.9 40.7 1.0

Iron binding site 2 out of 4 in 1xvd

Go back to Iron Binding Sites List in 1xvd
Iron binding site 2 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe529

b:78.5
occ:1.00
 ND1 A:HIS246 2.1 66.8 1.0
OE2 A:GLU209 2.4 71.2 1.0
OE1 A:GLU243 2.6 64.5 1.0
FE A:FE528 2.8 63.1 1.0
OE2 A:GLU243 2.8 62.8 1.0
CE1 A:HIS246 2.9 66.9 1.0
OE1 A:GLU144 3.0 44.0 1.0
CD A:GLU243 3.1 63.7 1.0
CG A:HIS246 3.2 66.1 1.0
CD A:GLU209 3.3 71.5 1.0
O A:HOH2861 3.5 47.1 1.0
CB A:HIS246 3.6 63.8 1.0
NE2 A:GLN140 3.7 42.2 1.0
CD A:GLU144 3.9 40.9 1.0
O A:HOH2862 4.0 52.4 1.0
OE2 A:GLU144 4.1 42.3 1.0
NE2 A:HIS246 4.1 67.0 1.0
CG A:GLU209 4.1 70.1 1.0
OE1 A:GLU209 4.1 73.5 1.0
CD2 A:HIS246 4.2 65.6 1.0
CE1 A:HIS147 4.5 34.7 1.0
ND1 A:HIS147 4.5 34.7 1.0
CD A:GLN140 4.5 43.8 1.0
CG A:GLU243 4.5 61.9 1.0
OE1 A:GLU114 4.8 61.1 1.0
CG A:GLN140 4.8 43.0 1.0
CB A:GLU209 4.9 67.2 1.0

Iron binding site 3 out of 4 in 1xvd

Go back to Iron Binding Sites List in 1xvd
Iron binding site 3 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe528

b:63.0
occ:1.00
 OE1 B:GLU114 1.9 55.6 1.0
ND1 B:HIS147 2.2 35.5 1.0
OE2 B:GLU144 2.4 44.0 1.0
FE B:FE529 2.6 72.9 1.0
O B:HOH2864 2.7 55.6 1.0
CD B:GLU114 2.9 51.0 1.0
O B:HOH2865 2.9 45.9 1.0
CE1 B:HIS147 3.0 36.4 1.0
OE2 B:GLU114 3.2 55.4 1.0
CD B:GLU144 3.2 42.3 1.0
CG B:HIS147 3.3 33.7 1.0
OE1 B:GLU144 3.3 42.3 1.0
CE1 B:HIS246 3.6 66.9 1.0
CB B:HIS147 3.7 32.9 1.0
ND1 B:HIS246 3.9 66.6 1.0
OE2 B:GLU243 4.1 62.4 1.0
NE2 B:HIS147 4.2 36.3 1.0
CG B:GLU114 4.2 48.3 1.0
OE1 B:GLU243 4.4 63.2 1.0
CD2 B:HIS147 4.4 34.1 1.0
CD B:GLU243 4.7 62.3 1.0
CG B:GLU144 4.7 40.5 1.0
CB B:GLU114 4.7 42.9 1.0
OE1 B:GLU209 4.8 68.2 1.0
CA B:GLU144 4.8 37.2 1.0
CG2 B:ILE239 4.8 36.7 1.0
NE2 B:HIS246 4.9 65.8 1.0
CA B:GLU114 4.9 40.9 1.0

Iron binding site 4 out of 4 in 1xvd

Go back to Iron Binding Sites List in 1xvd
Iron binding site 4 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Soluble Methane Monooxygenase Hydroxylase: 4-Fluorophenol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe529

b:72.9
occ:1.00
 ND1 B:HIS246 1.9 66.6 1.0
OE1 B:GLU243 2.5 63.2 1.0
CE1 B:HIS246 2.5 66.9 1.0
FE B:FE528 2.6 63.0 1.0
OE1 B:GLU144 2.7 42.3 1.0
OE1 B:GLU209 2.7 68.2 1.0
O B:HOH2864 3.1 55.6 1.0
OE2 B:GLU243 3.2 62.4 1.0
CG B:HIS246 3.2 65.6 1.0
CD B:GLU243 3.2 62.3 1.0
CD B:GLU209 3.4 68.7 1.0
O B:HOH2865 3.4 45.9 1.0
CD B:GLU144 3.5 42.3 1.0
OE2 B:GLU144 3.6 44.0 1.0
NE2 B:HIS246 3.8 65.8 1.0
CB B:HIS246 3.9 64.1 1.0
OE2 B:GLU209 4.1 67.4 1.0
CD2 B:HIS246 4.1 66.0 1.0
CG B:GLU209 4.1 68.8 1.0
ND1 B:HIS147 4.1 35.5 1.0
CE1 B:HIS147 4.2 36.4 1.0
OE1 B:GLU114 4.3 55.6 1.0
NE2 B:GLN140 4.4 49.4 1.0
CG B:GLU243 4.7 60.4 1.0
CD B:GLN140 4.7 48.8 1.0
CG B:GLN140 4.9 47.8 1.0
CG B:GLU144 5.0 40.5 1.0

Reference:

M.H.Sazinsky, S.J.Lippard. Product Bound Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath): Protein Motion in the Alpha-Subunit J.Am.Chem.Soc. V. 127 5814 2005.
ISSN: ISSN 0002-7863
PubMed: 15839679
DOI: 10.1021/JA044099B
Page generated: Wed Jul 16 22:12:23 2025

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