Atomistry » Iron » PDB 1fnq-1fz1 » 1fz1
Atomistry »
  Iron »
    PDB 1fnq-1fz1 »
      1fz1 »

Iron in PDB 1fz1: Methane Monooxygenase Hydroxylase, Form III Oxidized

Enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Oxidized

All present enzymatic activity of Methane Monooxygenase Hydroxylase, Form III Oxidized:
1.14.13.25;

Protein crystallography data

The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized, PDB code: 1fz1 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) 22.80 / 1.96
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.400, 171.970, 221.380, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 23.4

Other elements in 1fz1:

The structure of Methane Monooxygenase Hydroxylase, Form III Oxidized also contains other interesting chemical elements:

Calcium (Ca) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Methane Monooxygenase Hydroxylase, Form III Oxidized (pdb code 1fz1). 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 Oxidized, PDB code: 1fz1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1fz1

Go back to Iron Binding Sites List in 1fz1
Iron binding site 1 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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

b:25.7
occ:1.00
O A:HOH9273 1.9 40.7 1.0
OE1 A:GLU114 2.0 27.9 1.0
ND1 A:HIS147 2.2 21.7 1.0
OE2 A:GLU144 2.2 25.2 1.0
O A:HOH9187 2.4 24.8 1.0
O2 A:FMT9001 2.5 40.5 1.0
CD A:GLU114 3.0 27.7 1.0
CE1 A:HIS147 3.1 21.3 1.0
CD A:GLU144 3.1 23.0 1.0
FE A:FE5002 3.2 36.7 1.0
CG A:HIS147 3.3 20.2 1.0
C A:FMT9001 3.3 45.0 1.0
OE1 A:GLU144 3.3 24.0 1.0
OE2 A:GLU114 3.4 29.6 1.0
CB A:HIS147 3.6 18.5 1.0
O1 A:FMT9001 4.2 49.8 1.0
OE2 A:GLU243 4.2 48.4 1.0
NE2 A:HIS147 4.2 24.7 1.0
CD2 A:HIS147 4.3 23.9 1.0
CG A:GLU114 4.4 25.0 1.0
CE1 A:HIS246 4.4 27.0 1.0
ND1 A:HIS246 4.5 27.7 1.0
CG A:GLU144 4.6 17.5 1.0
OE1 A:GLU243 4.6 37.5 1.0
CB A:GLU114 4.7 21.0 1.0
CA A:GLU114 4.7 21.7 1.0
CA A:GLU144 4.7 18.4 1.0
OE2 A:GLU209 4.7 46.7 1.0
CG2 A:ILE239 4.8 22.5 1.0
CD A:GLU243 4.8 42.6 1.0

Iron binding site 2 out of 4 in 1fz1

Go back to Iron Binding Sites List in 1fz1
Iron binding site 2 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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

b:36.7
occ:1.00
OE2 A:GLU209 2.0 46.7 1.0
O A:HOH9273 2.0 40.7 1.0
ND1 A:HIS246 2.2 27.7 1.0
OE1 A:GLU243 2.4 37.5 1.0
OE1 A:GLU144 2.4 24.0 1.0
O2 A:FMT9001 2.5 40.5 1.0
CE1 A:HIS246 3.0 27.0 1.0
CD A:GLU209 3.1 46.8 1.0
CD A:GLU243 3.2 42.6 1.0
FE A:FE5001 3.2 25.7 1.0
OE2 A:GLU243 3.3 48.4 1.0
CG A:HIS246 3.3 28.4 1.0
CD A:GLU144 3.4 23.0 1.0
OE2 A:GLU144 3.7 25.2 1.0
C A:FMT9001 3.7 45.0 1.0
CB A:HIS246 3.8 30.0 1.0
NE2 A:GLN140 3.9 26.3 1.0
OE1 A:GLU209 3.9 47.6 1.0
CG A:GLU209 4.0 45.9 1.0
NE2 A:HIS246 4.2 27.9 1.0
O A:HOH9187 4.3 24.8 1.0
CD2 A:HIS246 4.4 26.9 1.0
O1 A:FMT9001 4.5 49.8 1.0
CD A:GLN140 4.5 26.5 1.0
CG A:GLU243 4.6 40.4 1.0
ND1 A:HIS147 4.6 21.7 1.0
CE1 A:HIS147 4.6 21.3 1.0
CG A:GLN140 4.7 25.5 1.0
CG A:GLU144 4.8 17.5 1.0
CB A:GLU209 4.9 42.4 1.0
OE1 A:GLU114 5.0 27.9 1.0

Iron binding site 3 out of 4 in 1fz1

Go back to Iron Binding Sites List in 1fz1
Iron binding site 3 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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

b:26.0
occ:1.00
O B:HOH5170 1.8 35.7 1.0
OE1 B:GLU114 2.0 25.6 1.0
OE2 B:GLU144 2.2 24.9 1.0
ND1 B:HIS147 2.2 18.9 1.0
O B:HOH5169 2.4 31.9 1.0
O B:HOH5293 2.7 36.4 1.0
CD B:GLU114 2.9 26.8 1.0
CD B:GLU144 3.1 23.2 1.0
CE1 B:HIS147 3.1 17.1 1.0
FE B:FE5004 3.2 36.6 1.0
CG B:HIS147 3.2 14.3 1.0
OE2 B:GLU114 3.3 32.9 1.0
OE1 B:GLU144 3.4 27.6 1.0
CB B:HIS147 3.6 19.5 1.0
OE2 B:GLU243 4.2 48.0 1.0
NE2 B:HIS147 4.3 21.0 1.0
CG B:GLU114 4.3 23.0 1.0
CD2 B:HIS147 4.3 17.0 1.0
CE1 B:HIS246 4.4 32.3 1.0
ND1 B:HIS246 4.5 29.6 1.0
CG B:GLU144 4.5 22.0 1.0
CA B:GLU144 4.6 19.3 1.0
CB B:GLU114 4.6 22.1 1.0
O B:HOH5294 4.7 45.1 1.0
OE1 B:GLU243 4.7 40.6 1.0
CA B:GLU114 4.7 21.7 1.0
CG2 B:ILE239 4.8 20.2 1.0
OE1 B:GLU209 4.8 42.6 1.0
CD B:GLU243 4.8 45.3 1.0
CB B:GLU144 4.9 18.4 1.0

Iron binding site 4 out of 4 in 1fz1

Go back to Iron Binding Sites List in 1fz1
Iron binding site 4 out of 4 in the Methane Monooxygenase Hydroxylase, Form III Oxidized


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

b:36.6
occ:1.00
O B:HOH5170 1.9 35.7 1.0
ND1 B:HIS246 2.2 29.6 1.0
OE1 B:GLU209 2.2 42.6 1.0
OE1 B:GLU243 2.3 40.6 1.0
OE1 B:GLU144 2.5 27.6 1.0
O B:HOH5293 2.8 36.4 1.0
CE1 B:HIS246 3.0 32.3 1.0
CD B:GLU209 3.0 45.3 1.0
CD B:GLU243 3.1 45.3 1.0
FE B:FE5003 3.2 26.0 1.0
OE2 B:GLU243 3.3 48.0 1.0
CG B:HIS246 3.3 29.7 1.0
CD B:GLU144 3.4 23.2 1.0
OE2 B:GLU144 3.6 24.9 1.0
CG B:GLU209 3.7 43.5 1.0
NE2 B:GLN140 3.7 22.9 1.0
CB B:HIS246 3.8 29.6 1.0
OE2 B:GLU209 3.8 46.0 1.0
O B:HOH5169 4.1 31.9 1.0
NE2 B:HIS246 4.2 29.9 1.0
CD2 B:HIS246 4.4 29.7 1.0
CD B:GLN140 4.5 28.9 1.0
ND1 B:HIS147 4.5 18.9 1.0
CG B:GLU243 4.6 41.7 1.0
CE1 B:HIS147 4.6 17.1 1.0
CG B:GLN140 4.7 24.8 1.0
CG B:GLU144 4.8 22.0 1.0
OE1 B:GLU114 4.9 25.6 1.0
O B:HOH5294 4.9 45.1 1.0
CB B:GLU209 4.9 43.3 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 05:32:25 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy