Chlorine in PDB 1hbn: Methyl-Coenzyme M Reductase

The structure of Methyl-Coenzyme M Reductase, PDB code: 1hbn was solved by U.Ermler, W.Grabarse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.16
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.720, 116.883, 122.582, 90.00, 92.02, 90.00
R / Rfree (%)	12.4 / 19

The structure of Methyl-Coenzyme M Reductase also contains other interesting chemical elements:

Nickel	(Ni)	2 atoms
Magnesium	(Mg)	18 atoms
Zinc	(Zn)	1 atom
Sodium	(Na)	10 atoms

The binding sites of Chlorine atom in the Methyl-Coenzyme M Reductase (pdb code 1hbn). 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, PDB code: 1hbn:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Methyl-Coenzyme M Reductase


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 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1446 b:20.3 occ:1.00 O B:HOH2126 3.0 25.7 1.0 O B:HOH2283 3.1 16.3 1.0 O B:HOH2349 3.1 21.3 1.0 NH2 B:ARG235 3.2 15.4 1.0 CB B:ALA300 3.7 14.4 1.0 CD B:ARG235 3.8 13.9 1.0 CB B:ARG235 3.9 13.7 1.0 CG B:ARG235 4.0 14.3 1.0 CZ B:ARG235 4.3 13.9 1.0 CD1 C:LEU248 4.4 52.0 1.0 NE B:ARG235 4.4 14.4 1.0 O B:HOH2166 4.5 59.0 1.0 O C:LEU248 4.7 53.8 1.0 O B:HOH2282 4.7 16.2 1.0 O B:ALA232 4.7 14.8 1.0 O B:HOH2346 4.7 51.0 1.0 CD2 C:LEU248 4.8 51.9 1.0 N B:MET236 4.8 13.6 1.0 OD1 B:ASP298 4.9 16.9 1.0 O B:HOH2058 4.9 43.5 1.0 CB C:LEU248 4.9 50.9 1.0 CA B:ALA300 5.0 14.3 1.0

Chlorine binding site 2 out of 2 in the Methyl-Coenzyme M Reductase


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 within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl1445 b:22.4 occ:1.00 O E:HOH2338 3.1 22.4 1.0 O E:HOH2126 3.1 30.3 1.0 O E:HOH2275 3.1 19.6 1.0 NH2 E:ARG235 3.2 18.0 1.0 CD E:ARG235 3.7 17.7 1.0 CB E:ALA300 3.7 17.5 1.0 CB E:ARG235 3.9 17.4 1.0 CG E:ARG235 3.9 17.4 1.0 CD1 F:LEU248 3.9 46.1 1.0 CZ E:ARG235 4.3 18.3 1.0 NE E:ARG235 4.5 18.0 1.0 CB F:LEU248 4.6 43.8 1.0 O F:LEU248 4.7 43.2 0.0 O E:HOH2277 4.8 19.4 1.0 O E:ALA232 4.8 17.8 1.0 CG F:LEU248 4.8 46.1 1.0 N E:MET236 4.8 15.7 1.0 OD1 E:ASP298 4.8 19.1 1.0

W.Grabarse, F.Mahlert, E.C.Duin, M.Goubeaud, S.Shima, R.K.Thauer, V.Lamzin, U.Ermler. On the Mechanism of Biological Methane Formation: Structural Evidence For Conformational Changes in Methyl-Coenzyme M Reductase Upon Substrate Binding J.Mol.Biol. V. 309 315 2001.
ISSN: ISSN 0022-2836
PubMed: 11491299
DOI: 10.1006/JMBI.2001.4647