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Molybdenum in PDB 4us8: Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Benzaldehyde

Enzymatic activity of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Benzaldehyde

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

Protein crystallography data

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Benzaldehyde, PDB code: 4us8 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) 124.04 / 1.49
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 143.229, 143.229, 162.250, 90.00, 90.00, 120.00
R / Rfree (%) 9.109 / 12.215

Other elements in 4us8:

The structure of Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Benzaldehyde 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 Benzaldehyde (pdb code 4us8). 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 Benzaldehyde, PDB code: 4us8:

Molybdenum binding site 1 out of 1 in 4us8

Go back to Molybdenum Binding Sites List in 4us8
Molybdenum binding site 1 out of 1 in the Aldehyde Oxidoreductase From Desulfovibrio Gigas (Mop), Soaked with Benzaldehyde


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 Benzaldehyde within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo921

b:7.7
occ:0.70
MO A:PCD921 0.0 7.7 0.7
OR1 A:PCD921 1.8 11.7 1.0
OM2 A:PCD921 1.9 13.0 1.0
OM1 A:PCD921 2.0 8.6 0.7
O1' A:HBX924 2.4 18.1 0.3
S7' A:PCD921 2.4 8.0 1.0
S8' A:PCD921 2.5 9.0 1.0
C1' A:HBX924 3.2 14.9 0.3
C7' A:PCD921 3.4 7.1 1.0
C8' A:PCD921 3.4 7.4 1.0
OE2 A:GLU869 3.7 8.1 1.0
CA A:GLY422 4.0 6.4 1.0
CA A:GLY696 4.1 7.3 1.0
CD A:GLU869 4.1 7.6 1.0
O A:HOH3013 4.1 19.3 0.7
N A:GLY697 4.3 6.9 1.0
N A:ARG533 4.4 6.3 1.0
CA A:ARG533 4.4 6.2 1.0
O A:SER695 4.5 7.7 1.0
N A:GLY422 4.5 6.1 1.0
CB A:ALA531 4.6 8.5 1.0
C1 A:HBX924 4.6 14.1 0.3
CG A:GLU869 4.6 7.4 1.0
OE1 A:GLU869 4.7 7.6 1.0
C A:GLY696 4.8 7.3 1.0
O A:PHE421 4.8 6.7 1.0
C6' A:PCD921 4.8 6.3 1.0
C A:PHE421 4.8 6.1 1.0
C9' A:PCD921 4.8 7.2 1.0
CE1 A:HIS653 4.9 7.4 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 Dec 15 05:19:14 2020

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