Atomistry » Potassium » PDB 5mrm-5s9l » 5n28
Atomistry »
  Potassium »
    PDB 5mrm-5s9l »
      5n28 »

Potassium in PDB 5n28: Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form

Enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form

All present enzymatic activity of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form, PDB code: 5n28 was solved by T.Wagner, C.E.Wegner, U.Ermler, S.Shima, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.43 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 103.680, 81.160, 154.950, 90.00, 107.80, 90.00
R / Rfree (%) 19.3 / 20.4

Other elements in 5n28:

The structure of Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form also contains other interesting chemical elements:

Nickel (Ni) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form (pdb code 5n28). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form, PDB code: 5n28:

Potassium binding site 1 out of 1 in 5n28

Go back to Potassium Binding Sites List in 5n28
Potassium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase III From Methanotorris Formicicus Monoclinic Form


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 III From Methanotorris Formicicus Monoclinic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K605

b:73.0
occ:1.00
 O A:CYS221 2.4 62.3 1.0
O A:GLY218 2.7 68.2 1.0
O D:CYS221 2.7 62.4 1.0
O A:ARG219 2.9 68.3 1.0
O D:ARG219 3.0 62.6 1.0
O D:GLY218 3.0 64.7 1.0
NH1 D:ARG105 3.5 60.8 1.0
C A:CYS221 3.6 62.5 1.0
C A:ARG219 3.6 69.3 1.0
C D:ARG219 3.7 63.0 1.0
NH2 A:ARG105 3.8 53.3 1.0
C A:GLY218 3.8 69.1 1.0
CA A:ARG219 3.9 65.7 1.0
C D:CYS221 3.9 62.7 1.0
CA D:ARG219 4.0 60.1 1.0
C D:GLY218 4.1 64.6 1.0
O A:HOH707 4.1 46.6 1.0
O D:HOH705 4.1 60.4 1.0
N A:ARG219 4.3 65.9 1.0
CA A:ASP222 4.3 57.0 1.0
N A:ASP222 4.3 58.0 1.0
CZ D:ARG105 4.4 68.8 1.0
N A:CYS221 4.4 61.2 1.0
CZ A:ARG105 4.4 73.7 1.0
C A:VAL220 4.5 66.3 1.0
N D:ARG219 4.5 60.6 1.0
NH2 D:ARG105 4.5 55.3 1.0
N A:VAL220 4.6 65.3 1.0
CA A:CYS221 4.6 59.5 1.0
CA D:ASP222 4.6 59.7 1.0
O A:VAL220 4.6 66.0 1.0
N D:ASP222 4.6 59.6 1.0
NH1 A:ARG105 4.6 67.3 1.0
C D:VAL220 4.7 63.1 1.0
N D:CYS221 4.7 59.2 1.0
O D:VAL220 4.8 62.3 1.0
N D:VAL220 4.8 59.4 1.0
CA D:CYS221 4.9 59.0 1.0

Reference:

T.Wagner, C.E.Wegner, J.Kahnt, U.Ermler, S.Shima. Phylogenetic and Structural Comparisons of the Three Types of Methyl Coenzyme M Reductase From Methanococcales and Methanobacteriales. J.Bacteriol. V. 199 2017.
ISSN: ESSN 1098-5530
PubMed: 28559298
DOI: 10.1128/JB.00197-17
Page generated: Mon Aug 12 14:19:00 2024

Last articles

Fe in 2YXO
Fe in 2YRS
Fe in 2YXC
Fe in 2YNM
Fe in 2YVJ
Fe in 2YP1
Fe in 2YU2
Fe in 2YU1
Fe in 2YQB
Fe in 2YOO
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy