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Molybdenum in PDB 3fah: Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas

Enzymatic activity of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas

All present enzymatic activity of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas:
1.2.99.7;

Protein crystallography data

The structure of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fah was solved by T.Santos-Silva, M.J.Romao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.98 / 1.72
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 142.560, 142.560, 161.880, 90.00, 90.00, 120.00
R / Rfree (%) 16 / 19.1

Other elements in 3fah:

The structure of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms
Iron (Fe) 4 atoms
Chlorine (Cl) 3 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas (pdb code 3fah). 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 Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas, PDB code: 3fah:

Molybdenum binding site 1 out of 1 in 3fah

Go back to Molybdenum Binding Sites List in 3fah
Molybdenum binding site 1 out of 1 in the Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Glycerol Inhibited Form of Aldehyde Oxidoreductase From Desulfovibrio Gigas within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo921

b:26.2
occ:1.00
 MO A:PCD921 0.0 26.2 1.0
OR1 A:PCD921 1.8 23.1 1.0
OM1 A:PCD921 2.1 20.7 1.0
O2 A:GOL912 2.1 33.7 1.0
S7' A:PCD921 2.3 16.1 1.0
S8' A:PCD921 2.4 16.9 1.0
C2 A:GOL912 2.7 35.4 1.0
C1 A:GOL912 3.1 36.9 1.0
C7' A:PCD921 3.3 15.2 1.0
C8' A:PCD921 3.3 15.0 1.0
OE1 A:GLU869 3.8 28.0 1.0
CA A:GLY422 3.9 24.9 1.0
C3 A:GOL912 4.1 33.8 1.0
CD A:GLU869 4.1 26.4 1.0
CA A:GLY696 4.2 25.3 1.0
N A:ARG533 4.3 24.7 1.0
CA A:ARG533 4.3 25.3 1.0
N A:GLY697 4.3 24.6 1.0
O3 A:GOL912 4.4 30.3 1.0
O A:SER695 4.4 25.9 1.0
N A:GLY422 4.4 24.9 1.0
O1 A:GOL912 4.5 39.7 1.0
CG A:GLU869 4.6 25.2 1.0
CB A:ALA531 4.6 26.1 1.0
OE2 A:GLU869 4.6 25.2 1.0
O A:PHE421 4.7 25.1 1.0
C A:PHE421 4.7 24.0 1.0
C6' A:PCD921 4.8 12.6 1.0
C9' A:PCD921 4.8 13.3 1.0
CE1 A:HIS653 4.8 26.7 1.0
C A:GLY696 4.8 25.9 1.0

Reference:

T.Santos-Silva, F.Ferroni, A.Thapper, J.Marangon, P.J.Gonzalez, A.C.Rizzi, I.Moura, J.J.Moura, M.J.Romao, C.D.Brondino. Kinetic, Structural, and Epr Studies Reveal That Aldehyde Oxidoreductase From Desulfovibrio Gigas Does Not Need A Sulfido Ligand For Catalysis and Give Evidence For A Direct Mo-C Interaction in A Biological System. J.Am.Chem.Soc. V. 131 7990 2009.
ISSN: ISSN 0002-7863
PubMed: 19459677
DOI: 10.1021/JA809448R
Page generated: Sun Oct 6 15:52:22 2024

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