Potassium in PDB 7nkg: Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution, PDB code: 7nkg was solved by M.Mueller, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.36 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 132.615, 148.177, 235.415, 90, 90, 90
R / Rfree (%) 17.3 / 19

Other elements in 7nkg:

The structure of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution also contains other interesting chemical elements:

Nickel (Ni) 4 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution (pdb code 7nkg). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution, PDB code: 7nkg:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 7nkg

Go back to Potassium Binding Sites List in 7nkg
Potassium binding site 1 out of 2 in the Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K602

b:16.3
occ:1.00
 O D:CYS236 2.7 15.5 1.0
O A:CYS236 2.8 14.4 1.0
O D:ARG234 2.8 14.9 1.0
O A:ARG234 2.8 16.0 1.0
O D:VAL233 3.0 15.6 1.0
O A:VAL233 3.0 15.2 1.0
NH1 A:ARG120 3.3 16.5 1.0
NH1 D:ARG120 3.3 17.1 1.0
C A:ARG234 3.6 15.4 1.0
C D:ARG234 3.6 15.1 1.0
C D:CYS236 3.8 15.1 1.0
C A:CYS236 3.8 14.3 1.0
CA A:ARG234 3.8 14.4 1.0
CA D:ARG234 3.8 15.1 1.0
O A:HOH786 4.0 18.3 1.0
O D:HOH786 4.0 19.6 1.0
CZ A:ARG120 4.0 18.5 1.0
C A:VAL233 4.0 14.8 1.0
C D:VAL233 4.0 15.0 1.0
CZ D:ARG120 4.1 19.6 1.0
NH2 A:ARG120 4.1 16.5 1.0
NH2 D:ARG120 4.2 17.1 1.0
N D:CYS236 4.4 14.4 1.0
N A:CYS236 4.4 14.6 1.0
N A:ARG234 4.4 15.1 1.0
N D:ARG234 4.4 15.1 1.0
CA D:ASP237 4.5 14.5 1.0
CA A:ASP237 4.5 14.1 1.0
N D:ASP237 4.5 14.3 1.0
N A:ASP237 4.6 13.4 1.0
C D:THR235 4.6 15.3 1.0
C A:THR235 4.6 15.2 1.0
N D:THR235 4.6 14.5 1.0
N A:THR235 4.6 14.5 1.0
CA D:CYS236 4.7 14.2 1.0
CA A:CYS236 4.7 14.7 1.0
O D:THR235 4.9 16.0 1.0
O A:THR235 4.9 16.0 1.0

Potassium binding site 2 out of 2 in 7nkg

Go back to Potassium Binding Sites List in 7nkg
Potassium binding site 2 out of 2 in the Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Methyl-Coenzyme M Reductase From Methermicoccus Shengliensis at 1.6-A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
G:K601

b:24.1
occ:1.00
 O J:CYS236 2.7 23.6 1.0
O J:ARG234 2.8 26.2 1.0
O G:CYS236 2.8 26.8 1.0
O G:ARG234 2.8 25.6 1.0
O J:VAL233 2.9 22.5 1.0
O G:VAL233 3.0 27.3 1.0
NH1 G:ARG120 3.3 26.8 1.0
NH1 J:ARG120 3.3 24.0 1.0
C J:ARG234 3.5 25.0 1.0
C G:ARG234 3.6 26.1 1.0
C J:CYS236 3.8 22.5 1.0
CA J:ARG234 3.8 23.9 1.0
C G:CYS236 3.8 26.3 1.0
CA G:ARG234 3.9 26.9 1.0
O G:HOH787 3.9 26.0 1.0
O J:HOH789 4.0 27.1 1.0
C J:VAL233 4.0 22.3 1.0
CZ G:ARG120 4.0 27.9 1.0
C G:VAL233 4.1 28.1 1.0
CZ J:ARG120 4.1 25.7 1.0
NH2 G:ARG120 4.1 26.6 1.0
NH2 J:ARG120 4.2 25.7 1.0
N J:CYS236 4.4 23.3 1.0
N J:ARG234 4.4 22.8 1.0
N G:ARG234 4.5 27.8 1.0
N G:CYS236 4.5 25.4 1.0
CA G:ASP237 4.5 26.4 1.0
CA J:ASP237 4.5 21.3 1.0
N J:ASP237 4.5 21.6 1.0
N G:ASP237 4.6 26.4 1.0
C J:THR235 4.6 24.5 1.0
N J:THR235 4.6 24.6 1.0
CA J:CYS236 4.7 23.0 1.0
C G:THR235 4.7 26.1 1.0
N G:THR235 4.7 26.4 1.0
CA G:CYS236 4.7 25.8 1.0
O J:THR235 4.9 25.1 1.0
O G:THR235 5.0 26.2 1.0

Reference:

J.M.Kurth, M.C.Muller, C.U.Welte, T.Wagner. Structural Insights Into the Methane-Generating Enzyme From A Methoxydotrophic Methanogen Reveal A Restrained Gallery of Post-Translational Modifications. Microorganisms V. 9 2021.
ISSN: ESSN 2076-2607
PubMed: 33919946
DOI: 10.3390/MICROORGANISMS9040837
Page generated: Sat Jul 10 16:27:29 2021

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