Atomistry » Tungsten » PDB 6sdr-7ax2 » 6sdv
Atomistry »
  Tungsten »
    PDB 6sdr-7ax2 »
      6sdv »

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: Wed Dec 16 02:39:13 2020

Last articles

Zn in 7M6U
Zn in 7NNG
Zn in 7NEE
Zn in 7NEU
Zn in 7M3K
Zn in 7KWD
Zn in 7KYH
Zn in 7KNG
Zn in 7KY2
Zn in 7KYF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy