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Tungsten in PDB 6sdr: W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Oxidized Form

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

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

Protein crystallography data

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Oxidized Form, PDB code: 6sdr 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) 48.36 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.593, 127.644, 148.213, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / 22.6

Other elements in 6sdr:

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Oxidized 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 - Oxidized Form (pdb code 6sdr). 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 - Oxidized Form, PDB code: 6sdr:

Tungsten binding site 1 out of 1 in 6sdr

Go back to Tungsten Binding Sites List in 6sdr
Tungsten binding site 1 out of 1 in the W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Oxidized 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 - Oxidized Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:W1110

b:26.2
occ:1.00
S A:H2S1109 2.3 27.5 1.0
S13 A:MGD1101 2.4 21.0 1.0
S12 A:MGD1101 2.4 23.0 1.0
S13 A:MGD1102 2.4 24.0 1.0
S12 A:MGD1102 2.5 20.0 1.0
SE A:SEC192 2.5 30.5 1.0
C13 A:MGD1101 3.4 19.3 1.0
C12 A:MGD1101 3.4 19.6 1.0
C13 A:MGD1102 3.5 25.2 1.0
C12 A:MGD1102 3.5 30.4 1.0
CB A:SEC192 3.6 24.1 1.0
NH2 A:ARG884 4.4 22.2 1.0
CA A:GLY442 4.4 19.0 1.0
NE2 A:GLN890 4.4 25.5 1.0
O A:GLN188 4.8 22.8 1.0
C14 A:MGD1101 4.9 17.2 1.0
C11 A:MGD1101 4.9 20.3 1.0
NE2 A:HIS193 4.9 32.2 1.0
OE1 A:GLN890 4.9 21.0 1.0
C14 A:MGD1102 4.9 25.0 1.0
C11 A:MGD1102 4.9 31.9 1.0
CA A:SEC192 4.9 30.5 1.0
CB A:GLN188 5.0 24.0 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: Wed Dec 16 02:39:13 2020

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