Chlorine in PDB 5a0y: 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;

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

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
Potassium	(K)	1 atom
Sodium	(Na)	2 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution, PDB code: 5a0y:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl 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:Cl565 b:24.1 occ:0.49 O A:HOH2403 2.2 14.0 0.5 NZ F:LYS153 2.7 15.0 0.3 O A:SER237 2.8 13.8 1.0 NZ F:LYS153 2.9 14.6 0.7 O A:HOH2292 3.3 11.3 1.0 O A:HOH2278 3.5 19.5 1.0 C A:SER237 3.7 12.5 1.0 OG A:SER237 3.8 11.3 1.0 O F:HOH2166 3.8 30.2 1.0 NZ A:LYS240 3.9 54.4 1.0 CA A:SER237 4.0 10.8 1.0 CE F:LYS153 4.1 13.4 0.3 O A:HOH2402 4.2 16.9 1.0 CG A:LYS240 4.2 36.3 1.0 CE F:LYS153 4.4 11.7 0.7 CB A:SER237 4.5 10.5 1.0 O A:HOH2279 4.6 12.7 1.0 CA A:LYS240 4.7 21.6 1.0 O F:HOH2193 4.8 31.3 1.0 CD F:LYS153 4.9 12.2 0.3 N A:ALA238 4.9 12.9 1.0 O A:ILE236 4.9 11.6 1.0 N A:LYS240 5.0 20.0 1.0 CE A:LYS240 5.0 50.9 1.0

Chlorine binding site 2 out of 2 in the Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Methyl-Coenzyme M Reductase From Methanothermobacter Marburgensis at 1.1 A Resolution within 5.0Å range: probe atom residue distance (Å) B Occ D:Cl559 b:26.0 occ:0.56 O D:HOH2393 2.2 14.7 0.6 O D:HOH2396 2.9 25.4 1.0 O D:HOH2401 2.9 42.6 1.0 N D:GLU298 3.3 13.0 1.0 CB D:GLU298 3.4 20.0 1.0 C D:ASN296 3.5 11.2 1.0 O D:ASN296 3.5 13.3 1.0 N D:ASP299 3.5 11.5 1.0 CA D:ASN296 3.6 9.5 1.0 CA D:GLU298 3.6 14.6 1.0 C D:GLU298 3.7 13.6 1.0 CB D:ASP299 3.9 12.5 1.0 N D:TYR297 4.0 14.4 1.0 O D:HOH2221 4.1 40.9 1.0 CG D:GLU298 4.2 28.0 1.0 CB D:ASN296 4.3 9.9 1.0 CA D:ASP299 4.3 11.0 1.0 C D:TYR297 4.3 16.7 1.0 O D:VAL295 4.4 11.3 0.7 O D:VAL295 4.5 10.0 0.3 O D:GLU298 4.6 15.5 1.0 OD1 D:ASN296 4.6 11.7 1.0 O D:HOH2403 4.8 24.4 1.0 N D:ASN296 4.8 9.9 1.0 CA D:TYR297 4.8 16.0 1.0

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