Atomistry » Iron » PDB 1fz2-1gek » 1fzh
Atomistry »
  Iron »
    PDB 1fz2-1gek »
      1fzh »

Iron in PDB 1fzh: Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas, PDB code: 1fzh 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) 29.00 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.270, 174.620, 223.000, 90.00, 90.00, 90.00
R / Rfree (%) 20.6 / 26

Other elements in 1fzh:

The structure of Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas also contains other interesting chemical elements:

Xenon (Xe) 11 atoms
Calcium (Ca) 4 atoms

Iron Binding Sites:

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

Iron binding site 1 out of 4 in 1fzh

Go back to Iron Binding Sites List in 1fzh
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5001

b:27.9
occ:1.00
O A:HOH9142 1.6 38.3 1.0
OE1 A:GLU114 2.0 30.6 1.0
ND1 A:HIS147 2.1 21.4 1.0
OE2 A:GLU144 2.5 23.2 1.0
O A:HOH9141 2.5 25.5 1.0
CE1 A:HIS147 3.0 22.9 1.0
CD A:GLU114 3.1 30.0 1.0
FE A:FE5002 3.1 31.6 1.0
CG A:HIS147 3.3 23.4 1.0
CD A:GLU144 3.3 23.9 1.0
OE1 A:GLU144 3.4 23.2 1.0
OE2 A:GLU114 3.5 32.5 1.0
CB A:HIS147 3.7 21.4 1.0
OE2 A:GLU243 4.0 45.9 1.0
NE2 A:HIS147 4.2 22.1 1.0
CE1 A:HIS246 4.3 33.9 1.0
CD2 A:HIS147 4.3 21.9 1.0
CG A:GLU114 4.4 30.0 1.0
ND1 A:HIS246 4.5 34.4 1.0
OE2 A:GLU209 4.5 40.8 1.0
CB A:GLU114 4.6 27.6 1.0
CG2 A:ILE239 4.7 33.2 1.0
CG A:GLU144 4.8 24.5 1.0
CA A:GLU114 4.8 26.6 1.0
CD A:GLU243 4.8 45.8 1.0
OE1 A:GLU243 4.8 45.3 1.0
CA A:GLU144 4.9 24.3 1.0

Iron binding site 2 out of 4 in 1fzh

Go back to Iron Binding Sites List in 1fzh
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe5002

b:31.6
occ:1.00
O A:HOH9142 1.5 38.3 1.0
OE2 A:GLU209 1.9 40.8 1.0
ND1 A:HIS246 2.2 34.4 1.0
OE1 A:GLU243 2.5 45.3 1.0
OE1 A:GLU144 2.7 23.2 1.0
OE2 A:GLU243 2.8 45.9 1.0
CE1 A:HIS246 2.8 33.9 1.0
CD A:GLU243 3.0 45.8 1.0
CD A:GLU209 3.0 40.8 1.0
FE A:FE5001 3.1 27.9 1.0
CG A:HIS246 3.3 33.4 1.0
CD A:GLU144 3.7 23.9 1.0
NE2 A:GLN140 3.7 20.9 1.0
OE1 A:GLU209 3.8 41.3 1.0
OE2 A:GLU144 3.9 23.2 1.0
CB A:HIS246 3.9 35.3 1.0
CG A:GLU209 3.9 39.4 1.0
NE2 A:HIS246 4.0 33.3 1.0
O A:HOH9141 4.1 25.5 1.0
CD2 A:HIS246 4.3 33.4 1.0
CG A:GLU243 4.5 44.4 1.0
ND1 A:HIS147 4.5 21.4 1.0
CE1 A:HIS147 4.5 22.9 1.0
CD A:GLN140 4.7 22.5 1.0
CB A:GLU209 4.8 36.6 1.0
OE1 A:GLU114 4.9 30.6 1.0

Iron binding site 3 out of 4 in 1fzh

Go back to Iron Binding Sites List in 1fzh
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5003

b:28.6
occ:1.00
O B:HOH9145 1.9 25.3 1.0
OE1 B:GLU114 2.0 30.8 1.0
OE2 B:GLU144 2.2 28.6 1.0
O B:HOH9144 2.2 29.2 1.0
ND1 B:HIS147 2.3 28.4 1.0
CD B:GLU114 3.0 32.4 1.0
CD B:GLU144 3.0 28.0 1.0
FE B:FE5004 3.1 36.3 1.0
CE1 B:HIS147 3.1 27.6 1.0
OE1 B:GLU144 3.2 26.3 1.0
OE2 B:GLU114 3.3 31.2 1.0
CG B:HIS147 3.4 27.8 1.0
CB B:HIS147 3.8 25.9 1.0
OE2 B:GLU243 4.1 45.8 1.0
NE2 B:HIS147 4.3 26.5 1.0
CG B:GLU114 4.4 31.4 1.0
OE1 B:GLU209 4.4 38.5 1.0
ND1 B:HIS246 4.4 44.7 1.0
CD2 B:HIS147 4.5 28.3 1.0
CE1 B:HIS246 4.5 44.4 1.0
OE1 B:GLU243 4.5 41.4 1.0
CG B:GLU144 4.5 25.6 1.0
CA B:GLU144 4.7 25.8 1.0
CD B:GLU243 4.7 44.5 1.0
CB B:GLU114 4.7 31.1 1.0
CA B:GLU114 4.8 30.9 1.0
CG2 B:ILE239 4.9 32.4 1.0
CB B:GLU144 4.9 25.0 1.0

Iron binding site 4 out of 4 in 1fzh

Go back to Iron Binding Sites List in 1fzh
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form II Pressurized with Xenon Gas


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 Pressurized with Xenon Gas within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe5004

b:36.3
occ:1.00
OE1 B:GLU209 1.8 38.5 1.0
O B:HOH9145 2.1 25.3 1.0
OE1 B:GLU243 2.3 41.4 1.0
ND1 B:HIS246 2.4 44.7 1.0
OE1 B:GLU144 2.4 26.3 1.0
CD B:GLU209 2.8 37.1 1.0
FE B:FE5003 3.1 28.6 1.0
CD B:GLU243 3.3 44.5 1.0
CE1 B:HIS246 3.3 44.4 1.0
CG B:HIS246 3.4 43.9 1.0
CD B:GLU144 3.4 28.0 1.0
OE2 B:GLU243 3.5 45.8 1.0
CG B:GLU209 3.6 37.6 1.0
CB B:HIS246 3.6 42.2 1.0
OE2 B:GLU209 3.7 36.3 1.0
OE2 B:GLU144 3.7 28.6 1.0
O B:HOH9144 3.9 29.2 1.0
NE2 B:GLN140 4.0 33.5 1.0
NE2 B:HIS246 4.5 45.2 1.0
CD2 B:HIS246 4.5 43.7 1.0
CD B:GLN140 4.6 33.1 1.0
CG B:GLU243 4.6 43.0 1.0
ND1 B:HIS147 4.7 28.4 1.0
CE1 B:HIS147 4.7 27.6 1.0
CB B:GLU209 4.8 37.8 1.0
CG B:GLU144 4.8 25.6 1.0
CG B:GLN140 4.8 32.8 1.0
OE1 B:GLU114 4.9 30.8 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 14:14:55 2020

Last articles

Zn in 7O75
Zn in 7O73
Zn in 7O4I
Zn in 7O72
Zn in 7O4J
Zn in 7NVR
Zn in 7NVY
Zn in 7NVZ
Zn in 7NW0
Zn in 7O4K
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy