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Iron in PDB 1fz4: Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris):
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris), PDB code: 1fz4 was solved by D.A.Whittington, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.70 / 2.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.890, 171.520, 221.690, 90.00, 90.00, 90.00
R / Rfree (%) 22.3 / 25.6

Other elements in 1fz4:

The structure of Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris) also contains other interesting chemical elements:

Calcium (Ca) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris) (pdb code 1fz4). 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 III Soaked at pH 8.5 (0.1 M Tris), PDB code: 1fz4:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz4

Go back to Iron Binding Sites List in 1fz4
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)


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 III Soaked at pH 8.5 (0.1 M Tris) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:47.8
occ:1.00
 O A:HOH6103 1.7 81.6 1.0
OE1 A:GLU114 2.1 49.9 1.0
ND1 A:HIS147 2.4 37.9 1.0
OE1 A:GLU144 2.6 48.8 1.0
O A:HOH6057 2.7 45.9 1.0
O2 A:FMT6001 3.0 60.2 1.0
FE A:FE5002 3.1 67.1 1.0
CD A:GLU114 3.1 47.5 1.0
CE1 A:HIS147 3.2 37.5 1.0
CD A:GLU144 3.4 46.4 1.0
CG A:HIS147 3.5 36.0 1.0
OE2 A:GLU114 3.5 49.0 1.0
OE2 A:GLU144 3.5 44.9 1.0
OE1 A:GLU243 3.8 64.4 1.0
C A:FMT6001 3.8 61.9 1.0
CB A:HIS147 3.8 32.1 1.0
OE2 A:GLU243 4.4 62.4 1.0
NE2 A:HIS147 4.4 38.6 1.0
CG A:GLU114 4.5 45.2 1.0
ND1 A:HIS246 4.5 59.7 1.0
CE1 A:HIS246 4.5 60.0 1.0
CD A:GLU243 4.5 63.6 1.0
CD2 A:HIS147 4.5 37.1 1.0
CA A:GLU114 4.7 40.4 1.0
CG2 A:ILE239 4.7 39.8 1.0
CB A:GLU114 4.7 42.1 1.0
O1 A:FMT6001 4.8 63.2 1.0
OE2 A:GLU209 4.8 66.9 1.0
CG A:GLU144 4.9 45.3 1.0
CA A:GLU144 5.0 40.2 1.0

Iron binding site 2 out of 4 in 1fz4

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Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)


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 III Soaked at pH 8.5 (0.1 M Tris) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:67.1
occ:1.00
 O A:HOH6103 1.8 81.6 1.0
OE2 A:GLU243 2.0 62.4 1.0
OE2 A:GLU209 2.1 66.9 1.0
ND1 A:HIS246 2.4 59.7 1.0
CD A:GLU243 2.8 63.6 1.0
OE2 A:GLU144 3.0 44.9 1.0
OE1 A:GLU243 3.0 64.4 1.0
FE A:FE5001 3.1 47.8 1.0
CD A:GLU209 3.1 65.3 1.0
CE1 A:HIS246 3.3 60.0 1.0
CG A:HIS246 3.4 59.8 1.0
CB A:HIS246 3.7 59.3 1.0
O2 A:FMT6001 3.7 60.2 1.0
CG A:GLU209 3.8 64.5 1.0
CD A:GLU144 3.9 46.4 1.0
OE1 A:GLU209 4.0 64.1 1.0
NE2 A:GLN140 4.0 46.7 1.0
OE1 A:GLU144 4.0 48.8 1.0
O A:HOH6057 4.1 45.9 1.0
CG A:GLU243 4.3 62.8 1.0
NE2 A:HIS246 4.4 59.0 1.0
CD2 A:HIS246 4.5 58.3 1.0
C A:FMT6001 4.6 61.9 1.0
CD A:GLN140 4.6 47.3 1.0
ND1 A:HIS147 4.7 37.9 1.0
CB A:GLU209 4.8 62.3 1.0
CE1 A:HIS147 4.8 37.5 1.0
O1 A:FMT6001 4.8 63.2 1.0
CG A:GLN140 4.8 48.0 1.0

Iron binding site 3 out of 4 in 1fz4

Go back to Iron Binding Sites List in 1fz4
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)


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 III Soaked at pH 8.5 (0.1 M Tris) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:48.2
occ:1.00
 O B:HOH5111 1.6 49.5 1.0
OE1 B:GLU114 1.8 43.9 1.0
ND1 B:HIS147 2.2 36.6 1.0
OE2 B:GLU144 2.7 36.4 1.0
CD B:GLU114 2.8 41.6 1.0
FE B:FE5004 3.0 59.8 1.0
OE2 B:GLU114 3.0 42.1 1.0
CE1 B:HIS147 3.1 36.4 1.0
CG B:HIS147 3.2 35.5 1.0
CB B:HIS147 3.5 35.2 1.0
CD B:GLU144 3.6 37.0 1.0
OE1 B:GLU144 3.8 37.6 1.0
OE2 B:GLU243 4.1 52.7 1.0
CG B:GLU114 4.2 40.9 1.0
NE2 B:HIS147 4.3 36.4 1.0
CE1 B:HIS246 4.3 63.3 1.0
CD2 B:HIS147 4.3 34.0 1.0
ND1 B:HIS246 4.4 64.1 1.0
CG2 B:ILE239 4.5 35.1 1.0
CB B:GLU114 4.6 39.9 1.0
CA B:GLU114 4.7 40.6 1.0
CA B:GLU144 4.8 37.4 1.0
OE1 B:GLU209 4.9 57.7 1.0
CG B:GLU144 5.0 38.0 1.0

Iron binding site 4 out of 4 in 1fz4

Go back to Iron Binding Sites List in 1fz4
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Soaked at pH 8.5 (0.1 M Tris)


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 III Soaked at pH 8.5 (0.1 M Tris) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:59.8
occ:1.00
 O B:HOH5111 1.6 49.5 1.0
ND1 B:HIS246 2.2 64.1 1.0
OE1 B:GLU209 2.3 57.7 1.0
OE1 B:GLU243 2.7 53.0 1.0
OE2 B:GLU243 2.8 52.7 1.0
OE1 B:GLU144 2.9 37.6 1.0
CE1 B:HIS246 2.9 63.3 1.0
FE B:FE5003 3.0 48.2 1.0
CD B:GLU243 3.1 53.8 1.0
CD B:GLU209 3.2 57.6 1.0
CG B:HIS246 3.3 63.4 1.0
CD B:GLU144 3.8 37.0 1.0
CG B:GLU209 3.8 57.1 1.0
OE2 B:GLU144 3.8 36.4 1.0
CB B:HIS246 3.8 63.0 1.0
OE2 B:GLU209 4.1 56.4 1.0
NE2 B:HIS246 4.1 63.1 1.0
ND1 B:HIS147 4.3 36.6 1.0
CD2 B:HIS246 4.4 63.3 1.0
NE2 B:GLN140 4.4 50.9 1.0
CE1 B:HIS147 4.5 36.4 1.0
CG B:GLU243 4.6 53.5 1.0
OE1 B:GLU114 4.6 43.9 1.0
CD B:GLN140 4.9 50.2 1.0
CB B:GLU209 5.0 55.3 1.0

Reference:

D.A.Whittington, S.J.Lippard. Crystal Structures of the Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) Demonstrating Geometrical Variability at the Dinuclear Iron Active Site. J.Am.Chem.Soc. V. 123 827 2001.
ISSN: ISSN 0002-7863
PubMed: 11456616
DOI: 10.1021/JA003240N
Page generated: Sat Aug 3 05:40:33 2024

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