Atomistry » Iron » PDB 1xvd-1y4q » 1xvd
Atomistry »
  Iron »
    PDB 1xvd-1y4q »
      1xvd »

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

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy