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Sodium in PDB 5a8w: Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution, PDB code: 5a8w 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) 48.66 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 110.391, 102.185, 118.739, 89.20, 93.97, 90.98
R / Rfree (%) 16.5 / 20.1

Other elements in 5a8w:

The structure of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution also contains other interesting chemical elements:

Nickel (Ni) 4 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution (pdb code 5a8w). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution, PDB code: 5a8w:

Sodium binding site 1 out of 1 in 5a8w

Go back to Sodium Binding Sites List in 5a8w
Sodium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Methyl-Coenzyme M Reductase II From Methanothermobacter Wolfeii at 1. 8 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Na1270

b:37.0
occ:1.00
 OD2 F:ASP229 2.2 40.6 1.0
N F:ALA226 2.9 18.7 1.0
CG F:ASP229 3.2 33.5 1.0
CA F:ILE225 3.4 13.4 1.0
C F:ILE225 3.6 16.1 1.0
CB F:ALA226 3.7 20.3 1.0
O F:ASN224 3.8 17.4 1.0
CA F:ALA226 3.9 15.2 1.0
CB F:ASP229 3.9 20.7 1.0
OD1 F:ASP229 4.1 34.9 1.0
CG2 F:ILE225 4.2 11.1 1.0
CB F:ILE225 4.3 11.6 1.0
N F:ILE225 4.4 13.7 1.0
C F:ASN224 4.5 14.7 1.0
O F:ALA226 4.5 11.3 1.0
O F:LYS222 4.5 16.5 1.0
C F:ALA226 4.7 14.0 1.0
O F:ILE225 4.8 12.8 1.0
CG1 F:ILE225 4.9 10.2 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: Mon Oct 7 19:51:21 2024

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