Chlorine in PDB 1hbm: Methyl-Coenzyme M Reductase Enzyme Product Complex

The structure of Methyl-Coenzyme M Reductase Enzyme Product Complex, PDB code: 1hbm 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)	10.00 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	82.000, 118.300, 122.800, 90.00, 92.00, 90.00
R / Rfree (%)	16.4 / 19.3

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

Nickel	(Ni)	2 atoms
Magnesium	(Mg)	5 atoms
Zinc	(Zn)	1 atom
Sodium	(Na)	9 atoms

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

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


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 Enzyme Product Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1446 b:22.0 occ:1.00 O B:HOH2109 2.9 24.1 1.0 O B:HOH2248 3.1 13.0 1.0 O B:HOH2305 3.2 21.0 1.0 NH2 B:ARG235 3.2 13.4 1.0 CD B:ARG235 3.7 14.0 1.0 CB B:ALA300 3.8 13.8 1.0 CB B:ARG235 3.8 13.0 1.0 CG B:ARG235 4.0 13.3 1.0 CZ B:ARG235 4.3 13.9 1.0 NE B:ARG235 4.4 13.9 1.0 O B:HOH2148 4.6 61.9 1.0 CD1 C:LEU248 4.7 43.2 1.0 O B:HOH2246 4.7 14.4 1.0 O B:HOH2302 4.7 53.7 1.0 CB C:LEU248 4.7 41.9 1.0 O B:ALA232 4.7 13.1 1.0 O B:HOH2007 4.7 47.4 1.0 N B:MET236 4.9 12.9 1.0 CD2 C:LEU248 4.9 43.0 1.0 OD1 B:ASP298 5.0 16.2 1.0

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


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 Enzyme Product Complex within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl1445 b:23.2 occ:1.00 O E:HOH2288 3.1 18.9 1.0 O E:HOH2237 3.2 20.3 1.0 O E:HOH2106 3.2 32.2 1.0 NH2 E:ARG235 3.2 18.4 1.0 CB E:ALA300 3.8 15.7 1.0 CD E:ARG235 3.9 18.5 1.0 CB E:ARG235 3.9 17.2 1.0 CG E:ARG235 4.0 18.3 1.0 CD1 F:LEU248 4.2 39.0 1.0 CZ E:ARG235 4.3 20.0 1.0 CB F:LEU248 4.4 37.5 1.0 O F:LEU248 4.5 43.2 0.0 NE E:ARG235 4.6 18.4 1.0 O E:HOH2239 4.7 18.2 1.0 O E:ALA232 4.8 19.4 1.0 OD1 E:ASP298 4.9 20.4 1.0 CG F:LEU248 5.0 38.3 1.0 N E:MET236 5.0 16.6 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