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Potassium in PDB 5a0y: Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution

Enzymatic activity of Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution

All present enzymatic activity of Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution:
2.8.4.1;

Protein crystallography data

The structure of Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution, PDB code: 5a0y was solved by T.Wagner, U.Ermler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.35 / 1.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 82.227, 118.300, 122.560, 90.00, 91.90, 90.00
R / Rfree (%) 11.1 / 12.9

Other elements in 5a0y:

The structure of Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution also contains other interesting chemical elements:

Nickel (Ni) 2 atoms
Magnesium (Mg) 16 atoms
Chlorine (Cl) 2 atoms
Sodium (Na) 2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution (pdb code 5a0y). 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 From Methanothermobacter Marburgensis at 1.1 A Resolution, PDB code: 5a0y:

Potassium binding site 1 out of 1 in 5a0y

Go back to Potassium Binding Sites List in 5a0y
Potassium binding site 1 out of 1 in the Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 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 Methanothermobacter Marburgensis at 1.1 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K561

b:9.3
occ:1.00
 O D:CYS218 2.7 5.6 1.0
O A:CYS218 2.8 5.6 1.0
O A:ARG216 2.8 5.7 1.0
O D:ARG216 2.8 5.9 1.0
O D:SER215 3.3 6.1 1.0
O A:SER215 3.4 5.8 1.0
NH1 D:ARG102 3.4 6.0 1.0
NH1 A:ARG102 3.5 6.2 1.0
C D:ARG216 3.6 5.7 1.0
C A:ARG216 3.6 4.8 1.0
O A:HOH2390 3.8 6.7 1.0
O A:HOH2224 3.8 6.5 1.0
C D:CYS218 3.8 5.3 1.0
C A:CYS218 3.8 5.4 1.0
CA D:ARG216 3.9 5.7 1.0
CA A:ARG216 3.9 5.2 1.0
CZ D:ARG102 4.0 5.7 1.0
CZ A:ARG102 4.0 5.5 1.0
NH2 D:ARG102 4.0 6.0 1.0
NH2 A:ARG102 4.0 6.2 1.0
C D:SER215 4.4 5.6 1.0
N D:CYS218 4.4 5.4 1.0
N A:CYS218 4.4 5.3 1.0
C A:SER215 4.4 5.1 1.0
C D:THR217 4.5 5.3 1.0
C A:THR217 4.5 5.4 1.0
CA A:ASP219 4.6 5.5 1.0
N D:ARG216 4.6 5.6 1.0
CA D:ASP219 4.6 5.5 1.0
N D:ASP219 4.6 5.8 1.0
N A:ASP219 4.6 5.6 1.0
N A:ARG216 4.6 5.6 1.0
N D:THR217 4.7 5.4 1.0
N A:THR217 4.7 5.0 1.0
CA D:CYS218 4.7 5.5 1.0
CA A:CYS218 4.7 5.1 1.0
O A:THR217 4.8 5.5 1.0
O D:THR217 4.8 5.8 1.0
NE D:ARG102 4.9 5.7 1.0
NE A:ARG102 5.0 5.9 1.0

Reference:

T.Wagner, J.Kahnt, U.Ermler, S.Shima. Didehydroaspartate Modification in Methyl-Coenzyme M Reductase Catalyzing Methane Formation. Angew.Chem.Int.Ed.Engl. V. 55 10630 2016.
ISSN: ISSN 1433-7851
PubMed: 27467699
DOI: 10.1002/ANIE.201603882
Page generated: Mon Aug 12 12:50:48 2024

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