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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: Sat Aug 9 09:35:04 2025

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