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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

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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: Tue Aug 5 16:22:57 2025

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