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Iron in PDB 1fz9: Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane

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

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

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane, PDB code: 1fz9 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) 30.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.220, 172.220, 221.190, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26

Other elements in 1fz9:

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

Iodine (I) 8 atoms
Calcium (Ca) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane (pdb code 1fz9). 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 Iodoethane, PDB code: 1fz9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz9

Go back to Iron Binding Sites List in 1fz9
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane


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 Iodoethane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:38.2
occ:1.00
 ND1 A:HIS147 2.2 34.3 1.0
OE1 A:GLU114 2.3 47.8 1.0
O A:HOH9192 2.4 42.5 1.0
OE2 A:GLU144 2.4 44.8 1.0
FE A:FE5002 2.9 45.5 1.0
CE1 A:HIS147 2.9 38.0 1.0
OE2 A:GLU243 3.1 49.3 1.0
CD A:GLU114 3.2 44.0 1.0
CD A:GLU144 3.2 41.9 1.0
CG A:HIS147 3.3 34.7 1.0
OE1 A:GLU144 3.3 37.1 1.0
OE2 A:GLU114 3.4 45.5 1.0
CB A:HIS147 3.8 36.1 1.0
CE1 A:HIS246 4.0 47.6 1.0
NE2 A:HIS147 4.1 37.6 1.0
CD A:GLU243 4.2 52.4 1.0
ND1 A:HIS246 4.2 47.6 1.0
CD2 A:HIS147 4.3 34.4 1.0
CG A:GLU114 4.6 42.5 1.0
OE2 A:GLU209 4.7 43.1 1.0
CG2 A:ILE239 4.7 27.2 1.0
CG A:GLU144 4.7 40.6 1.0
OE1 A:GLU243 4.7 44.0 1.0
CA A:GLU144 4.8 36.6 1.0
CB A:GLU114 4.9 32.8 1.0
CA A:GLU114 5.0 36.4 1.0

Iron binding site 2 out of 4 in 1fz9

Go back to Iron Binding Sites List in 1fz9
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane


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 Iodoethane within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:45.5
occ:1.00
 OE2 A:GLU209 2.1 43.1 1.0
OE2 A:GLU243 2.2 49.3 1.0
ND1 A:HIS246 2.3 47.6 1.0
OE1 A:GLU243 2.5 44.0 1.0
CD A:GLU243 2.7 52.4 1.0
OE1 A:GLU144 2.8 37.1 1.0
FE A:FE5001 2.9 38.2 1.0
CE1 A:HIS246 3.0 47.6 1.0
CD A:GLU209 3.1 45.5 1.0
CG A:HIS246 3.4 48.5 1.0
CD A:GLU144 3.7 41.9 1.0
NE2 A:GLN140 3.7 39.7 1.0
CG A:GLU209 3.7 45.5 1.0
CB A:HIS246 3.8 48.3 1.0
OE2 A:GLU144 3.9 44.8 1.0
O A:HOH9192 3.9 42.5 1.0
OE1 A:GLU209 4.1 42.0 1.0
CG A:GLU243 4.2 51.0 1.0
NE2 A:HIS246 4.2 45.3 1.0
CD2 A:HIS246 4.4 45.6 1.0
ND1 A:HIS147 4.5 34.3 1.0
CE1 A:HIS147 4.5 38.0 1.0
CB A:GLU209 4.6 47.4 1.0
CD A:GLN140 4.7 39.4 1.0
OE1 A:GLU114 4.7 47.8 1.0
CG A:GLN140 5.0 35.3 1.0

Iron binding site 3 out of 4 in 1fz9

Go back to Iron Binding Sites List in 1fz9
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane


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 Iodoethane within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:39.8
occ:1.00
 O B:HOH9151 1.7 41.4 1.0
OE1 B:GLU114 1.8 34.6 1.0
OE2 B:GLU144 2.2 31.4 1.0
ND1 B:HIS147 2.2 35.8 1.0
O B:HOH9150 2.6 42.1 1.0
CD B:GLU114 2.8 37.4 1.0
FE B:FE5004 2.9 44.2 1.0
CE1 B:HIS147 3.1 38.6 1.0
OE2 B:GLU114 3.2 42.5 1.0
CD B:GLU144 3.2 34.3 1.0
CG B:HIS147 3.3 38.8 1.0
OE1 B:GLU144 3.5 42.1 1.0
CB B:HIS147 3.6 37.9 1.0
OE2 B:GLU243 4.1 49.4 1.0
CG B:GLU114 4.2 35.0 1.0
CE1 B:HIS246 4.2 59.0 1.0
NE2 B:HIS147 4.3 37.5 1.0
CD2 B:HIS147 4.4 36.5 1.0
OE2 B:GLU209 4.4 56.4 1.0
ND1 B:HIS246 4.4 58.6 1.0
CB B:GLU114 4.5 38.3 1.0
CA B:GLU144 4.5 38.5 1.0
CG B:GLU144 4.6 34.7 1.0
CA B:GLU114 4.6 38.8 1.0
OE1 B:GLU243 4.7 47.2 1.0
CG2 B:ILE239 4.7 33.2 1.0
CD B:GLU243 4.8 53.2 1.0
CB B:GLU144 4.9 35.0 1.0

Iron binding site 4 out of 4 in 1fz9

Go back to Iron Binding Sites List in 1fz9
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Cocrystallized with Iodoethane


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 Iodoethane within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:44.2
occ:1.00
 OE2 B:GLU209 1.8 56.4 1.0
O B:HOH9151 1.9 41.4 1.0
ND1 B:HIS246 2.2 58.6 1.0
OE1 B:GLU243 2.3 47.2 1.0
OE1 B:GLU144 2.7 42.1 1.0
CE1 B:HIS246 2.9 59.0 1.0
FE B:FE5003 2.9 39.8 1.0
CD B:GLU209 3.0 55.5 1.0
CD B:GLU243 3.1 53.2 1.0
OE2 B:GLU243 3.2 49.4 1.0
CG B:HIS246 3.4 56.2 1.0
CD B:GLU144 3.5 34.3 1.0
OE2 B:GLU144 3.5 31.4 1.0
CG B:GLU209 3.8 54.1 1.0
OE1 B:GLU209 3.9 48.5 1.0
CB B:HIS246 3.9 52.1 1.0
O B:HOH9150 4.0 42.1 1.0
NE2 B:HIS246 4.1 57.4 1.0
NE2 B:GLN140 4.2 49.2 1.0
CD2 B:HIS246 4.4 54.9 1.0
ND1 B:HIS147 4.4 35.8 1.0
CE1 B:HIS147 4.5 38.6 1.0
OE1 B:GLU114 4.6 34.6 1.0
CG B:GLU243 4.6 51.9 1.0
CD B:GLN140 4.7 48.5 1.0
CB B:GLU209 4.9 53.6 1.0
CG B:GLN140 4.9 43.9 1.0
CG B:GLU144 5.0 34.7 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: Sat Aug 3 05:40:33 2024

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