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Magnesium in PDB 5a8k: Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution, PDB code: 5a8k was solved by T.Wagner, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.47 / 1.41
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 84.140, 150.540, 187.090, 90.00, 90.00, 90.00
R / Rfree (%) 11.4 / 14

Other elements in 5a8k:

The structure of Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Potassium (K) 5 atoms
Calcium (Ca) 12 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution (pdb code 5a8k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution, PDB code: 5a8k:

Magnesium binding site 1 out of 1 in 5a8k

Go back to Magnesium Binding Sites List in 5a8k
Magnesium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Methyl-Coenzyme M Reductase From Methanothermobacter Wolfeii at 1.4 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg251

b:14.7
occ:1.00
 O F:HOH2221 2.1 25.6 1.0
O F:HOH2251 2.3 33.1 1.0
O F:VAL219 2.3 12.1 1.0
O F:HOH2219 2.4 30.0 1.0
O F:HOH2218 2.4 16.5 1.0
O F:HOH2224 3.4 28.6 1.0
C F:VAL219 3.5 11.3 1.0
O F:GLY221 4.2 12.4 1.0
CG2 F:VAL219 4.3 13.3 1.0
O F:HOH2220 4.4 36.8 1.0
CA F:VAL219 4.4 11.6 1.0
N F:ASP220 4.5 10.8 1.0
CA F:ASP220 4.5 11.2 1.0
O F:HOH2227 4.8 14.4 1.0
O F:HOH2237 4.8 17.3 1.0
O F:HOH2236 4.9 37.3 1.0
C F:ASP220 4.9 11.9 1.0
N F:GLY221 5.0 10.3 1.0
CB F:VAL219 5.0 12.3 1.0

Reference:

T.Wagner, J.Kahnt, U.Ermler, S.Shima. Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation. Angew.Chem.Int.Ed.Engl. V. 55 10630 2016.
ISSN: ISSN 1433-7851
PubMed: 27467699
DOI: 10.1002/ANIE.201603882
Page generated: Sun Sep 29 00:20:33 2024

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