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Tungsten in PDB 5t5i: Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A

Enzymatic activity of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A

All present enzymatic activity of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A:
1.2.99.5;

Protein crystallography data

The structure of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A, PDB code: 5t5i was solved by T.Wagner, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.49 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 121.644, 174.576, 205.425, 90.00, 90.00, 90.00
R / Rfree (%) 15.2 / 17.2

Other elements in 5t5i:

The structure of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms
Potassium (K) 18 atoms
Zinc (Zn) 4 atoms
Iron (Fe) 88 atoms
Calcium (Ca) 2 atoms
Sodium (Na) 5 atoms

Tungsten Binding Sites:

The binding sites of Tungsten atom in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A (pdb code 5t5i). This binding sites where shown within 5.0 Angstroms radius around Tungsten atom.
In total 2 binding sites of Tungsten where determined in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A, PDB code: 5t5i:
Jump to Tungsten binding site number: 1; 2;

Tungsten binding site 1 out of 2 in 5t5i

Go back to Tungsten Binding Sites List in 5t5i
Tungsten binding site 1 out of 2 in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 1 of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A within 5.0Å range:
probe atom residue distance (Å) B Occ
B:W502

b:29.1
occ:1.00
S12 B:MGD503 2.5 18.5 1.0
S B:H2S505 2.5 20.9 1.0
S13 B:MGD504 2.5 22.0 1.0
S13 B:MGD503 2.5 20.9 1.0
S12 B:MGD504 2.6 19.5 1.0
SG B:CYS118 2.7 21.3 1.0
CB B:CYS118 3.2 17.9 1.0
C12 B:MGD503 3.3 19.2 1.0
C13 B:MGD503 3.4 16.5 1.0
C13 B:MGD504 3.4 20.8 1.0
C12 B:MGD504 3.4 18.9 1.0
NH1 D:ARG9 3.9 21.6 1.0
CA B:GLY289 4.2 20.7 1.0
CA B:CYS118 4.4 18.6 1.0
NE2 B:HIS290 4.6 25.3 1.0
CD2 B:HIS290 4.6 25.3 1.0
C11 B:MGD503 4.7 21.8 1.0
N B:GLY289 4.7 20.8 1.0
C14 B:MGD504 4.8 20.8 1.0
C11 B:MGD504 4.8 19.8 1.0
C14 B:MGD503 4.8 20.7 1.0
N B:HIS290 4.9 20.2 1.0
SD B:MET254 4.9 21.3 1.0
OG1 B:THR114 4.9 22.3 1.0
CZ D:ARG9 4.9 27.5 1.0

Tungsten binding site 2 out of 2 in 5t5i

Go back to Tungsten Binding Sites List in 5t5i
Tungsten binding site 2 out of 2 in the Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A


Mono view


Stereo pair view

A full contact list of Tungsten with other atoms in the W binding site number 2 of Tungsten-Containing Formylmethanofuran Dehydrogenase From Methanothermobacter Wolfeii, Orthorhombic Form at 1.9 A within 5.0Å range:
probe atom residue distance (Å) B Occ
J:W502

b:25.9
occ:1.00
S J:H2S505 2.5 19.6 1.0
S12 J:MGD504 2.5 16.6 1.0
S13 J:MGD503 2.5 17.0 1.0
S13 J:MGD504 2.5 16.9 1.0
S12 J:MGD503 2.6 17.0 1.0
SG J:CYS118 2.7 18.0 1.0
CB J:CYS118 3.2 15.4 1.0
C12 J:MGD504 3.3 16.6 1.0
C13 J:MGD504 3.3 11.4 1.0
C13 J:MGD503 3.4 18.0 1.0
C12 J:MGD503 3.4 15.4 1.0
NH1 L:ARG9 3.9 18.5 1.0
CA J:GLY289 4.2 19.2 1.0
CA J:CYS118 4.4 16.8 1.0
NE2 J:HIS290 4.6 21.2 1.0
CD2 J:HIS290 4.6 21.7 1.0
C11 J:MGD504 4.7 21.0 1.0
N J:GLY289 4.7 18.9 1.0
C14 J:MGD503 4.8 19.7 1.0
C14 J:MGD504 4.8 14.8 1.0
N J:HIS290 4.9 16.7 1.0
C11 J:MGD503 4.9 16.1 1.0
CZ L:ARG9 4.9 24.3 1.0
OG1 J:THR114 4.9 19.4 1.0
SD J:MET254 4.9 19.2 1.0
C J:GLY289 5.0 22.1 1.0

Reference:

T.Wagner, U.Ermler, S.Shima. The Methanogenic CO2 Reducing-and-Fixing Enzyme Is Bifunctional and Contains 46 [4FE-4S] Clusters. Science V. 354 114 2016.
ISSN: ESSN 1095-9203
PubMed: 27846502
DOI: 10.1126/SCIENCE.AAF9284
Page generated: Wed Dec 16 02:35:27 2020

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