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Tungsten in PDB 6sdv: W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form

Enzymatic activity of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form

All present enzymatic activity of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form:
1.2.1.2;

Protein crystallography data

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form, PDB code: 6sdv was solved by A.R.Oliveira, C.Mota, C.Mourato, R.M.Domingos, M.F.A.Santos, D.Gesto, B.Guigliarelli, T.Santos-Silva, M.J.Romao, I.C.Pereira, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.76 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.885, 128.560, 149.629, 90.00, 90.00, 90.00
R / Rfree (%) 15.9 / 19.7

Other elements in 6sdv:

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form also contains other interesting chemical elements:

Iron (Fe) 16 atoms

Tungsten Binding Sites:

The binding sites of Tungsten atom in the W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form (pdb code 6sdv). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total only one binding site of Tungsten was determined in the W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form, PDB code: 6sdv:

Tungsten binding site 1 out of 1 in 6sdv

Go back to Tungsten Binding Sites List in 6sdv
Tungsten binding site 1 out of 1 in the W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Formate Reduced Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:W1104

b:22.4
occ:1.00
 S13 A:MGD1101 2.3 17.6 1.0
S12 A:MGD1101 2.4 16.2 1.0
S12 A:MGD1102 2.4 23.1 1.0
S13 A:MGD1102 2.5 22.7 1.0
S A:H2S1105 2.5 23.0 1.0
SE A:SEC192 2.5 31.3 1.0
C13 A:MGD1101 3.3 14.2 1.0
C12 A:MGD1101 3.3 16.1 1.0
C13 A:MGD1102 3.4 18.0 1.0
C12 A:MGD1102 3.4 19.2 1.0
CB A:SEC192 3.5 23.5 1.0
NH2 A:ARG884 4.0 21.9 1.0
CA A:GLY442 4.5 17.5 1.0
NE2 A:GLN890 4.6 27.5 1.0
O A:HOH1475 4.6 20.9 1.0
C14 A:MGD1101 4.7 13.2 1.0
C11 A:MGD1101 4.8 16.3 1.0
CB A:GLN188 4.8 31.9 1.0
C14 A:MGD1102 4.8 19.6 1.0
CA A:SEC192 4.8 23.3 1.0
C11 A:MGD1102 4.9 20.6 1.0
N A:SEC192 5.0 27.1 1.0
O A:GLN188 5.0 27.1 1.0

Reference:

A.R.Oliveira, C.Mota, C.Mourato, R.M.Domingos, M.F.A.Santos, D.Gesto, B.Guigliarelli, T.Santos-Silva, M.J.Romao, I.C.Pereira. Towards the Mechanistic Understanding of Enzymatic CO2 Reduction Acs Catalysis 2020.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.0C00086
Page generated: Sat Oct 12 10:02:34 2024

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