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Tungsten in PDB 8rcc: W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min

Enzymatic activity of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min

All present enzymatic activity of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min:
1.2.1.2;

Protein crystallography data

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min, PDB code: 8rcc was solved by G.Vilela-Alves, P.Carpentier, R.R.Manuel, I.C.Pereira, M.J.Romao, C.Mota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 95.84 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 64.81, 124.401, 150.307, 90, 90, 90
R / Rfree (%) 19.4 / 24.4

Other elements in 8rcc:

The structure of W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min 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 - Aerobic Soaked with 48 Bar CO2 For 1 Min (pdb code 8rcc). 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 - Aerobic Soaked with 48 Bar CO2 For 1 Min, PDB code: 8rcc:

Tungsten binding site 1 out of 1 in 8rcc

Go back to Tungsten Binding Sites List in 8rcc
Tungsten binding site 1 out of 1 in the W-Formate Dehydrogenase From Desulfovibrio Vulgaris - Aerobic Soaked with 48 Bar CO2 For 1 Min


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 - Aerobic Soaked with 48 Bar CO2 For 1 Min within 5.0Å range:
probe atom residue distance (Å) B Occ
A:W1105

b:30.8
occ:1.00
 O1 A:OXY1131 1.9 33.8 1.0
S13 A:MGD1102 2.3 26.5 1.0
O2 A:OXY1131 2.4 32.5 1.0
S12 A:MGD1102 2.4 29.8 1.0
S13 A:MGD1101 2.5 27.3 1.0
S12 A:MGD1101 2.5 26.6 1.0
S A:H2S1104 2.8 43.9 1.0
C13 A:MGD1102 3.4 25.3 1.0
C12 A:MGD1102 3.4 28.7 1.0
C13 A:MGD1101 3.4 22.5 1.0
C12 A:MGD1101 3.5 22.6 1.0
SE A:SEC192 3.7 75.8 1.0
NH2 A:ARG884 4.2 21.3 1.0
O2 A:CO21112 4.3 50.3 1.0
C A:CO21112 4.4 56.2 1.0
CA A:GLY442 4.7 22.4 1.0
O1 A:CO21112 4.7 63.0 1.0
C14 A:MGD1102 4.8 23.5 1.0
O A:GLN188 4.8 28.1 1.0
C11 A:MGD1102 4.9 30.1 1.0
C14 A:MGD1101 4.9 23.1 1.0
C11 A:MGD1101 4.9 22.9 1.0

Reference:

G.Vilela-Alves, R.R.Manuel, A.Viegas, P.Carpentier, F.Biaso, B.Guigliarelli, I.C.Pereira, M.J.Romao, C.Mota. Substrate-Dependent Oxidative Inactivation of A W-Dependent Formate Dehydrogenase Involving Selenocysteine Displacement Chem Sci 2024.
ISSN: ESSN 2041-6539
Page generated: Tue Aug 19 16:45:58 2025

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