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Potassium in PDB 5n1q: Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution, PDB code: 5n1q 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) 45.63 / 1.90
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 111.811, 77.224, 145.458, 90.00, 107.01, 90.00
R / Rfree (%) 16.9 / 19

Other elements in 5n1q:

The structure of Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Magnesium (Mg) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution (pdb code 5n1q). 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 Methanothermococcus Thermolithotrophicus at 1.9 A Resolution, PDB code: 5n1q:

Potassium binding site 1 out of 1 in 5n1q

Go back to Potassium Binding Sites List in 5n1q
Potassium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase III From Methanothermococcus Thermolithotrophicus at 1.9 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 III From Methanothermococcus Thermolithotrophicus at 1.9 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K603

b:24.2
occ:1.00
 O A:CYS222 2.7 23.5 1.0
O D:CYS222 2.7 22.4 1.0
O D:GLY219 2.8 25.1 1.0
O A:GLY219 2.8 21.5 1.0
O D:ARG220 2.9 27.3 1.0
O A:ARG220 2.9 23.4 1.0
C D:ARG220 3.6 26.4 1.0
C A:ARG220 3.6 24.3 1.0
NH2 D:ARG106 3.7 19.9 1.0
NH2 A:ARG106 3.7 18.5 1.0
C D:CYS222 3.8 23.6 1.0
C A:CYS222 3.8 23.6 1.0
CA D:ARG220 3.8 22.1 1.0
C D:GLY219 3.9 26.2 1.0
CA A:ARG220 3.9 21.4 1.0
C A:GLY219 3.9 24.4 1.0
O D:HOH821 4.0 28.1 1.0
O A:HOH779 4.0 26.6 1.0
N D:ARG220 4.3 22.6 1.0
CZ D:ARG106 4.3 31.5 1.0
CZ A:ARG106 4.3 28.8 1.0
N A:ARG220 4.4 21.9 1.0
NH1 D:ARG106 4.4 18.4 1.0
NH1 A:ARG106 4.4 16.5 1.0
N D:CYS222 4.5 21.9 1.0
N A:CYS222 4.5 20.7 1.0
CA D:ASP223 4.6 20.0 1.0
CA A:ASP223 4.6 19.6 1.0
N D:ASP223 4.6 19.8 1.0
N A:ASP223 4.6 20.2 1.0
C D:VAL221 4.6 25.7 1.0
C A:VAL221 4.6 23.8 1.0
N D:VAL221 4.7 22.5 1.0
N A:VAL221 4.7 20.9 1.0
CA D:CYS222 4.7 21.0 1.0
CA A:CYS222 4.7 19.9 1.0
O D:VAL221 4.8 26.3 1.0
O A:VAL221 4.8 22.2 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 14:18:58 2024

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