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Iron in PDB 1fz8: Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane, PDB code: 1fz8 was solved by D.A.Whittington, A.C.Rosenzweig, C.A.Frederick, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.50 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.170, 171.990, 221.330, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 25

Other elements in 1fz8:

The structure of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane also contains other interesting chemical elements:

Bromine (Br) 20 atoms
Calcium (Ca) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane (pdb code 1fz8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane, PDB code: 1fz8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz8

Go back to Iron Binding Sites List in 1fz8
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


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, Form II Cocrystallized with Dibromomethane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:27.2
occ:1.00
 OE1 A:GLU114 2.1 35.5 1.0
ND1 A:HIS147 2.1 18.8 1.0
OE2 A:GLU144 2.3 26.2 1.0
O A:HOH9253 2.3 36.1 1.0
O A:HOH9112 2.4 36.7 1.0
CE1 A:HIS147 3.0 21.3 1.0
CD A:GLU114 3.0 31.5 1.0
FE A:FE5002 3.1 37.0 1.0
CG A:HIS147 3.2 20.3 1.0
OE2 A:GLU114 3.3 36.3 1.0
CD A:GLU144 3.3 27.3 1.0
CB A:HIS147 3.6 21.0 1.0
OE1 A:GLU144 3.6 25.4 1.0
NE2 A:HIS147 4.2 22.3 1.0
OE2 A:GLU243 4.2 49.6 1.0
CD2 A:HIS147 4.3 21.9 1.0
CE1 A:HIS246 4.3 34.3 1.0
CG A:GLU114 4.4 31.4 1.0
ND1 A:HIS246 4.5 34.4 1.0
OE1 A:GLU243 4.6 44.5 1.0
CG2 A:ILE239 4.6 22.1 1.0
CG A:GLU144 4.7 22.6 1.0
CA A:GLU114 4.7 27.8 1.0
CB A:GLU114 4.8 26.4 1.0
CA A:GLU144 4.8 21.1 1.0
O A:HOH9221 4.8 68.2 1.0
CD A:GLU243 4.8 48.7 1.0
OE2 A:GLU209 5.0 42.1 1.0

Iron binding site 2 out of 4 in 1fz8

Go back to Iron Binding Sites List in 1fz8
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


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, Form II Cocrystallized with Dibromomethane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:37.0
occ:1.00
 O A:HOH9253 2.0 36.1 1.0
OE2 A:GLU209 2.1 42.1 1.0
ND1 A:HIS246 2.3 34.4 1.0
OE1 A:GLU243 2.3 44.5 1.0
OE1 A:GLU144 2.7 25.4 1.0
CE1 A:HIS246 3.0 34.3 1.0
FE A:FE5001 3.1 27.2 1.0
CD A:GLU243 3.2 48.7 1.0
CD A:GLU209 3.3 39.7 1.0
CG A:HIS246 3.4 34.8 1.0
OE2 A:GLU243 3.5 49.6 1.0
CD A:GLU144 3.5 27.3 1.0
OE2 A:GLU144 3.6 26.2 1.0
CB A:HIS246 3.9 35.5 1.0
CG A:GLU209 4.0 40.0 1.0
NE2 A:GLN140 4.1 26.9 1.0
O A:HOH9112 4.2 36.7 1.0
OE1 A:GLU209 4.2 39.9 1.0
NE2 A:HIS246 4.2 33.4 1.0
CD2 A:HIS246 4.4 33.6 1.0
ND1 A:HIS147 4.5 18.8 1.0
CE1 A:HIS147 4.5 21.3 1.0
CG A:GLU243 4.6 45.4 1.0
CD A:GLN140 4.8 26.1 1.0
OE1 A:GLU114 4.9 35.5 1.0
CG A:GLN140 4.9 22.9 1.0
CB A:GLU209 5.0 33.8 1.0
CG A:GLU144 5.0 22.6 1.0

Iron binding site 3 out of 4 in 1fz8

Go back to Iron Binding Sites List in 1fz8
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:25.6
occ:1.00
 O B:HOH9114 2.0 26.7 1.0
OE1 B:GLU114 2.1 20.7 1.0
ND1 B:HIS147 2.3 18.1 1.0
O B:HOH9115 2.3 28.8 1.0
OE2 B:GLU144 2.3 29.3 1.0
FE B:FE5004 3.0 33.3 1.0
CD B:GLU114 3.1 23.1 1.0
CE1 B:HIS147 3.2 19.1 1.0
CD B:GLU144 3.2 27.2 1.0
CG B:HIS147 3.3 15.6 1.0
OE1 B:GLU144 3.4 27.2 1.0
OE2 B:GLU114 3.4 24.6 1.0
CB B:HIS147 3.6 19.1 1.0
OE2 B:GLU243 4.1 40.8 1.0
NE2 B:HIS147 4.3 18.3 1.0
CE1 B:HIS246 4.4 38.8 1.0
CD2 B:HIS147 4.4 11.5 1.0
ND1 B:HIS246 4.4 37.4 1.0
CG B:GLU114 4.5 23.3 1.0
CA B:GLU144 4.6 23.4 1.0
OE1 B:GLU243 4.6 29.3 1.0
CG B:GLU144 4.6 27.0 1.0
CB B:GLU114 4.7 21.8 1.0
OE1 B:GLU209 4.8 28.1 1.0
CG2 B:ILE239 4.8 16.5 1.0
CA B:GLU114 4.8 23.3 1.0
CD B:GLU243 4.8 39.5 1.0

Iron binding site 4 out of 4 in 1fz8

Go back to Iron Binding Sites List in 1fz8
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Dibromomethane within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:33.3
occ:1.00
 O B:HOH9114 1.9 26.7 1.0
ND1 B:HIS246 2.2 37.4 1.0
OE1 B:GLU209 2.3 28.1 1.0
OE1 B:GLU243 2.3 29.3 1.0
OE1 B:GLU144 2.5 27.2 1.0
FE B:FE5003 3.0 25.6 1.0
CE1 B:HIS246 3.0 38.8 1.0
CD B:GLU209 3.1 32.8 1.0
CD B:GLU243 3.2 39.5 1.0
CG B:HIS246 3.4 37.5 1.0
OE2 B:GLU243 3.4 40.8 1.0
CD B:GLU144 3.4 27.2 1.0
OE2 B:GLU144 3.6 29.3 1.0
CG B:GLU209 3.8 31.9 1.0
CB B:HIS246 3.8 35.7 1.0
NE2 B:GLN140 3.9 29.4 1.0
OE2 B:GLU209 4.0 29.2 1.0
O B:HOH9115 4.1 28.8 1.0
NE2 B:HIS246 4.2 37.9 1.0
CD2 B:HIS246 4.4 38.1 1.0
ND1 B:HIS147 4.5 18.1 1.0
CE1 B:HIS147 4.6 19.1 1.0
CD B:GLN140 4.6 30.0 1.0
CG B:GLU243 4.7 36.2 1.0
CG B:GLN140 4.7 30.0 1.0
CG B:GLU144 4.8 27.0 1.0
OE1 B:GLU114 4.9 20.7 1.0
CB B:GLU209 5.0 34.5 1.0

Reference:

D.A.Whittington, A.C.Rosenzweig, C.A.Frederick, S.J.Lippard. Xenon and Halogenated Alkanes Track Putative Substrate Binding Cavities in the Soluble Methane Monooxygenase Hydroxylase. Biochemistry V. 40 3476 2001.
ISSN: ISSN 0006-2960
PubMed: 11297413
DOI: 10.1021/BI0022487
Page generated: Sun Dec 13 14:14:51 2020

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