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Molybdenum in PDB 4us9: Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde

Enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde

All present enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde:
1.2.99.7;

Protein crystallography data

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde, PDB code: 4us9 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) 124.51 / 1.40
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 143.766, 143.766, 162.544, 90.00, 90.00, 120.00
R / Rfree (%) 9.343 / 11.696

Other elements in 4us9:

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde also contains other interesting chemical elements:

Magnesium (Mg) 4 atoms
Iron (Fe) 4 atoms
Chlorine (Cl) 2 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde (pdb code 4us9). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde, PDB code: 4us9:

Molybdenum binding site 1 out of 1 in 4us9

Go back to Molybdenum Binding Sites List in 4us9
Molybdenum binding site 1 out of 1 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with 3-Phenylpropionaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo921

b:12.8
occ:0.50
 MO A:PCD921 0.0 12.8 0.5
OM1 A:PCD921 1.9 18.2 1.0
OM2 A:PCD921 2.0 12.9 0.5
OR1 A:PCD921 2.1 13.2 1.0
S7' A:PCD921 2.4 7.2 1.0
S8' A:PCD921 2.5 10.1 1.0
O A:HOH3359 2.9 20.4 0.5
C7' A:PCD921 3.4 6.2 1.0
C8' A:PCD921 3.4 6.8 1.0
OE2 A:GLU869 3.9 5.9 1.0
CA A:GLY696 4.0 6.2 1.0
CA A:GLY422 4.0 5.1 1.0
O A:HOH3162 4.2 12.1 1.0
O A:SER695 4.2 6.1 1.0
CD A:GLU869 4.3 5.3 1.0
N A:GLY697 4.3 5.3 1.0
N A:GLY422 4.5 4.7 1.0
N A:ARG533 4.5 4.2 1.0
CA A:ARG533 4.6 4.2 1.0
CB A:ALA531 4.7 6.6 1.0
C A:GLY696 4.7 6.1 1.0
CG A:GLU869 4.8 5.0 1.0
CE1 A:HIS653 4.8 6.6 1.0
OE1 A:GLU869 4.8 5.9 1.0
C9' A:PCD921 4.8 6.5 1.0
O A:PHE421 4.8 5.1 1.0
C A:PHE421 4.8 4.5 1.0
C6' A:PCD921 4.8 5.4 1.0
N A:GLY696 5.0 6.0 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: Sun Oct 6 16:13:19 2024

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