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Iron in PDB 1xvc: Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure

Enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure

All present enzymatic activity of Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure:
1.14.13.25;

Protein crystallography data

The structure of Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure, PDB code: 1xvc 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) 29.79 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.411, 171.031, 221.434, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 23.4

Other elements in 1xvc:

The structure of Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure also contains other interesting chemical elements:

Bromine (Br) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol Soaked Structure (pdb code 1xvc). 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: 8-Bromooctanol Soaked Structure, PDB code: 1xvc:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1xvc

Go back to Iron Binding Sites List in 1xvc
Iron binding site 1 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol 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: 8-Bromooctanol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1330

b:28.8
occ:1.00
 O A:HOH1850 1.9 35.1 1.0
OE1 A:GLU114 2.0 30.5 1.0
OE2 A:GLU144 2.1 26.4 1.0
O A:HOH1707 2.1 29.2 1.0
ND1 A:HIS147 2.2 23.9 1.0
O A:HOH1851 2.4 31.7 1.0
CD A:GLU114 3.0 29.8 1.0
CE1 A:HIS147 3.0 23.2 1.0
FE A:FE935 3.0 39.9 1.0
CD A:GLU144 3.1 24.3 1.0
OE2 A:GLU114 3.2 32.8 1.0
CG A:HIS147 3.3 22.8 1.0
OE1 A:GLU144 3.3 26.9 1.0
CB A:HIS147 3.7 22.8 1.0
OE2 A:GLU243 3.9 44.0 1.0
NE2 A:HIS147 4.2 24.3 1.0
CE1 A:HIS246 4.3 34.5 1.0
CD2 A:HIS147 4.3 23.4 1.0
CG A:GLU114 4.3 28.4 1.0
OE1 A:GLU243 4.4 37.8 1.0
ND1 A:HIS246 4.5 34.0 1.0
CG A:GLU144 4.5 24.7 1.0
CD A:GLU243 4.6 40.4 1.0
CA A:GLU144 4.7 22.9 1.0
CG2 A:ILE239 4.7 25.8 1.0
CB A:GLU114 4.7 23.8 1.0
CA A:GLU114 4.7 25.4 1.0
OE2 A:GLU209 4.8 46.5 1.0
CB A:GLU144 4.9 21.6 1.0

Iron binding site 2 out of 4 in 1xvc

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Iron binding site 2 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol 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: 8-Bromooctanol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe935

b:39.9
occ:1.00
 O A:HOH1850 2.0 35.1 1.0
OE2 A:GLU209 2.1 46.5 1.0
OE1 A:GLU243 2.2 37.8 1.0
ND1 A:HIS246 2.2 34.0 1.0
OE1 A:GLU144 2.4 26.9 1.0
O A:HOH1851 2.6 31.7 1.0
CE1 A:HIS246 3.0 34.5 1.0
CD A:GLU243 3.0 40.4 1.0
FE A:FE1330 3.0 28.8 1.0
OE2 A:GLU243 3.1 44.0 1.0
CD A:GLU209 3.2 46.4 1.0
CD A:GLU144 3.3 24.3 1.0
CG A:HIS246 3.4 33.1 1.0
OE2 A:GLU144 3.5 26.4 1.0
CB A:HIS246 3.8 33.3 1.0
NE2 A:GLN140 3.9 25.9 1.0
O A:HOH1707 4.0 29.2 1.0
CG A:GLU209 4.0 45.0 1.0
OE1 A:GLU209 4.1 46.4 1.0
NE2 A:HIS246 4.2 32.5 1.0
CD2 A:HIS246 4.4 31.8 1.0
CG A:GLU243 4.4 39.9 1.0
ND1 A:HIS147 4.5 23.9 1.0
CE1 A:HIS147 4.5 23.2 1.0
CD A:GLN140 4.6 28.1 1.0
CG A:GLU144 4.7 24.7 1.0
OE1 A:GLU114 4.8 30.5 1.0
CG A:GLN140 4.9 26.5 1.0
CB A:GLU209 5.0 41.5 1.0

Iron binding site 3 out of 4 in 1xvc

Go back to Iron Binding Sites List in 1xvc
Iron binding site 3 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol 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: 8-Bromooctanol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1328

b:38.9
occ:1.00
 O B:HOH2244 1.8 34.5 1.0
OE1 B:GLU209 2.0 44.1 1.0
ND1 B:HIS246 2.1 38.4 1.0
OE1 B:GLU243 2.3 35.6 1.0
OE1 B:GLU144 2.4 27.5 1.0
O B:HOH2273 2.6 25.6 1.0
CE1 B:HIS246 2.8 37.4 1.0
FE B:FE1327 3.0 27.6 1.0
CD B:GLU209 3.1 43.7 1.0
CD B:GLU243 3.2 39.3 1.0
CG B:HIS246 3.3 37.9 1.0
CD B:GLU144 3.3 27.5 1.0
OE2 B:GLU243 3.4 42.2 1.0
OE2 B:GLU144 3.5 25.2 1.0
CG B:GLU209 3.7 44.2 1.0
CB B:HIS246 3.9 37.7 1.0
NE2 B:GLN140 3.9 30.1 1.0
OE2 B:GLU209 4.0 43.0 1.0
NE2 B:HIS246 4.0 37.7 1.0
O B:HOH2169 4.1 28.4 1.0
CD2 B:HIS246 4.3 37.8 1.0
ND1 B:HIS147 4.5 26.7 1.0
O B:HOH2274 4.5 49.0 1.0
CE1 B:HIS147 4.6 26.7 1.0
CD B:GLN140 4.6 32.5 1.0
CG B:GLU243 4.6 37.3 1.0
OE1 B:GLU114 4.7 27.9 1.0
CG B:GLU144 4.7 25.9 1.0
CG B:GLN140 4.8 30.2 1.0
CB B:GLU209 5.0 42.3 1.0

Iron binding site 4 out of 4 in 1xvc

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Iron binding site 4 out of 4 in the Soluble Methane Monooxygenase Hydroxylase: 8-Bromooctanol 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: 8-Bromooctanol Soaked Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1327

b:27.6
occ:1.00
 O B:HOH2244 1.7 34.5 1.0
OE1 B:GLU114 2.0 27.9 1.0
OE2 B:GLU144 2.2 25.2 1.0
ND1 B:HIS147 2.2 26.7 1.0
O B:HOH2169 2.4 28.4 1.0
O B:HOH2273 2.5 25.6 1.0
FE B:FE1328 3.0 38.9 1.0
CD B:GLU114 3.0 28.4 1.0
CE1 B:HIS147 3.1 26.7 1.0
CD B:GLU144 3.1 27.5 1.0
CG B:HIS147 3.3 25.5 1.0
OE1 B:GLU144 3.4 27.5 1.0
OE2 B:GLU114 3.4 33.2 1.0
CB B:HIS147 3.7 24.2 1.0
OE2 B:GLU243 4.2 42.2 1.0
CE1 B:HIS246 4.2 37.4 1.0
O B:HOH2274 4.2 49.0 1.0
NE2 B:HIS147 4.3 27.8 1.0
CG B:GLU114 4.4 28.0 1.0
CD2 B:HIS147 4.4 25.6 1.0
ND1 B:HIS246 4.4 38.4 1.0
OE1 B:GLU243 4.5 35.6 1.0
CG B:GLU144 4.5 25.9 1.0
CB B:GLU114 4.6 27.4 1.0
CA B:GLU144 4.6 26.3 1.0
CG2 B:ILE239 4.7 24.5 1.0
CA B:GLU114 4.7 26.9 1.0
OE1 B:GLU209 4.8 44.1 1.0
CD B:GLU243 4.8 39.3 1.0
CB B:GLU144 4.9 26.2 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: Sat Aug 3 17:01:33 2024

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