Atomistry » Iron » PDB 4ur2-4wgz » 4usa
Atomistry »
  Iron »
    PDB 4ur2-4wgz »
      4usa »

Iron in PDB 4usa: Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde

Enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde

All present enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde:
1.2.99.7;

Protein crystallography data

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde, PDB code: 4usa was solved by H.D.Correia, M.J.Romao, T.Santos-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 123.97 / 1.13
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 143.143, 143.143, 161.954, 90.00, 90.00, 120.00
R / Rfree (%) 10.165 / 12.172

Other elements in 4usa:

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde also contains other interesting chemical elements:

Molybdenum (Mo) 1 atom
Magnesium (Mg) 4 atoms
Chlorine (Cl) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde (pdb code 4usa). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde, PDB code: 4usa:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 4usa

Go back to Iron Binding Sites List in 4usa
Iron binding site 1 out of 4 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:9.0
occ:1.00
 FE1 A:FES908 0.0 9.0 1.0
S2 A:FES908 2.3 9.2 1.0
S1 A:FES908 2.3 9.5 1.0
SG A:CYS45 2.3 9.3 1.0
SG A:CYS40 2.4 10.0 1.0
FE2 A:FES908 2.7 8.8 1.0
CB A:CYS45 3.4 9.5 1.0
N A:CYS40 3.5 9.2 1.0
N A:CYS45 3.5 9.6 1.0
CB A:CYS40 3.6 10.4 1.0
N A:GLU41 3.8 9.5 1.0
CA A:CYS45 3.8 9.3 1.0
CA A:CYS40 3.9 9.8 1.0
N A:GLY46 4.0 8.8 1.0
C A:CYS45 4.2 8.3 1.0
N A:GLN44 4.2 9.2 1.0
C A:CYS40 4.3 9.6 1.0
SG A:CYS60 4.3 10.0 1.0
N A:ALA47 4.4 8.1 1.0
N A:GLY43 4.4 10.3 1.0
N A:GLY39 4.5 8.7 1.0
C A:GLY39 4.5 9.5 1.0
N A:GLN42 4.6 10.8 1.0
C A:GLN44 4.6 9.8 1.0
SG A:CYS48 4.7 9.2 1.0
CA A:GLY39 4.7 10.1 1.0
O A:HOH2134 4.7 17.5 1.0
CA A:GLU41 4.8 10.3 1.0
CA A:GLY43 4.8 10.8 1.0
C A:GLY43 4.9 10.2 1.0
CB A:ALA47 4.9 9.0 1.0
CA A:GLY46 5.0 9.1 1.0
CA A:GLN44 5.0 9.8 1.0

Iron binding site 2 out of 4 in 4usa

Go back to Iron Binding Sites List in 4usa
Iron binding site 2 out of 4 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe908

b:8.8
occ:1.00
 FE2 A:FES908 0.0 8.8 1.0
S2 A:FES908 2.2 9.2 1.0
S1 A:FES908 2.2 9.5 1.0
SG A:CYS48 2.3 9.2 1.0
SG A:CYS60 2.3 10.0 1.0
FE1 A:FES908 2.7 9.0 1.0
CB A:CYS60 3.2 9.7 1.0
CB A:CYS48 3.5 8.8 1.0
N A:CYS60 4.2 9.4 1.0
N A:CYS48 4.3 7.8 1.0
CA A:CYS60 4.3 9.7 1.0
N A:GLY43 4.3 10.3 1.0
CB A:ARG58 4.3 9.8 1.0
SG A:CYS40 4.4 10.0 1.0
CA A:CYS48 4.5 7.9 1.0
CG A:ARG58 4.5 11.5 1.0
CA A:GLY43 4.6 10.8 1.0
N A:GLU41 4.6 9.5 1.0
SG A:CYS45 4.6 9.3 1.0
CA A:GLU41 4.8 10.3 1.0
N A:GLY46 4.9 8.8 1.0
N A:GLN42 4.9 10.8 1.0
N A:ALA47 4.9 8.1 1.0

Iron binding site 3 out of 4 in 4usa

Go back to Iron Binding Sites List in 4usa
Iron binding site 3 out of 4 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe909

b:7.2
occ:1.00
 FE1 A:FES909 0.0 7.2 1.0
S1 A:FES909 2.2 7.7 1.0
S2 A:FES909 2.2 7.5 1.0
SG A:CYS103 2.3 8.0 1.0
SG A:CYS137 2.4 7.2 1.0
FE2 A:FES909 2.7 7.1 1.0
CB A:CYS137 3.4 7.5 1.0
CB A:CYS103 3.4 7.4 1.0
CA A:CYS137 3.8 7.2 1.0
O A:HOH2295 4.2 8.7 1.0
N A:CYS103 4.2 7.1 1.0
N A:ARG138 4.2 6.7 1.0
CB A:CYS139 4.3 7.0 1.0
N A:CYS139 4.4 6.9 1.0
CA A:CYS103 4.4 7.2 1.0
SG A:CYS139 4.4 8.1 1.0
C A:CYS137 4.4 7.1 1.0
CG2 A:THR140 4.6 7.7 1.0
SG A:CYS100 4.6 7.0 1.0
O A:ALA136 4.8 7.8 1.0
CA A:CYS139 4.9 7.0 1.0

Iron binding site 4 out of 4 in 4usa

Go back to Iron Binding Sites List in 4usa
Iron binding site 4 out of 4 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Trans-Cinnamaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe909

b:7.1
occ:1.00
 FE2 A:FES909 0.0 7.1 1.0
S1 A:FES909 2.2 7.7 1.0
S2 A:FES909 2.3 7.5 1.0
SG A:CYS100 2.3 7.0 1.0
SG A:CYS139 2.3 8.1 1.0
FE1 A:FES909 2.7 7.2 1.0
CB A:CYS139 3.3 7.0 1.0
CB A:CYS100 3.4 7.2 1.0
N A:CYS100 3.7 6.7 1.0
O A:HOH2907 3.9 8.1 1.0
CA A:CYS100 3.9 6.8 1.0
N A:GLY101 4.0 6.9 1.0
N A:CYS139 4.1 6.9 1.0
CA A:CYS139 4.3 7.0 1.0
C A:CYS100 4.3 7.0 1.0
SG A:CYS137 4.4 7.2 1.0
N A:PHE102 4.4 7.0 1.0
SG A:CYS103 4.6 8.0 1.0
C A:GLN99 4.8 6.9 1.0
CB A:GLN99 4.8 7.2 1.0
N A:ARG138 4.9 6.7 1.0
N A:CYS103 4.9 7.1 1.0
CA A:GLY101 5.0 7.1 1.0

Reference:

H.D.Correia, J.Marangon, C.D.Brondino, J.J.G.Moura, M.J.Romao, P.J.Gonzalez, T.Santos-Silva. Aromatic Aldehydes at the Active Site of Aldehyde Oxidoreductase From Desulfovibrio Gigas: Reactivity and Molecular Details of the Enzyme-Substrate and Enzyme- Product Interaction. J.Biol.Inorg.Chem. 2014.
ISSN: ESSN 1432-1327
PubMed: 25261288
DOI: 10.1007/S00775-014-1196-4
Page generated: Mon Aug 5 14:05:32 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy