Atomistry » Tungsten » PDB 6sdr-8bql » 6sdr
Atomistry »
  Tungsten »
    PDB 6sdr-8bql »
      6sdr »

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: Sat Oct 12 10:02:34 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy