Atomistry » Potassium » PDB 7loo-7ny1 » 7nkg
Atomistry »
  Potassium »
    PDB 7loo-7ny1 »
      7nkg »

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: Mon Aug 12 19:32:56 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy