Chlorine in PDB 1hbo: Methyl-Coenzyme M Reductase Mcr-RED1-Silent

The structure of Methyl-Coenzyme M Reductase Mcr-RED1-Silent, PDB code: 1hbo was solved by W.Grabarse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.78
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.700, 117.300, 122.400, 90.00, 92.00, 90.00
R / Rfree (%)	17.7 / 21.3

The structure of Methyl-Coenzyme M Reductase Mcr-RED1-Silent also contains other interesting chemical elements:

Nickel	(Ni)	2 atoms
Magnesium	(Mg)	4 atoms
Zinc	(Zn)	1 atom
Sodium	(Na)	8 atoms

The binding sites of Chlorine atom in the Methyl-Coenzyme M Reductase Mcr-RED1-Silent (pdb code 1hbo). 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 Mcr-RED1-Silent, PDB code: 1hbo:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Methyl-Coenzyme M Reductase Mcr-RED1-Silent


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 Mcr-RED1-Silent within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1446 b:25.5 occ:1.00 O B:HOH2111 3.0 27.1 1.0 O B:HOH2255 3.0 17.5 1.0 O B:HOH2312 3.2 22.9 1.0 NH2 B:ARG235 3.2 15.3 1.0 CD B:ARG235 3.7 16.9 1.0 CB B:ARG235 3.8 15.3 1.0 CB B:ALA300 3.8 15.4 1.0 CG B:ARG235 3.9 16.7 1.0 CZ B:ARG235 4.2 16.6 1.0 NE B:ARG235 4.4 16.2 1.0 O B:HOH2309 4.5 40.6 1.0 CB C:LEU248 4.6 41.4 1.0 O B:ALA232 4.7 16.8 1.0 CD1 C:LEU248 4.7 41.6 1.0 O B:HOH2253 4.8 16.0 1.0 N B:MET236 4.8 14.4 1.0 OD1 B:ASP298 4.9 20.3 1.0 O B:HOH2146 4.9 64.0 1.0 CA B:ARG235 5.0 15.3 1.0

Chlorine binding site 2 out of 2 in the Methyl-Coenzyme M Reductase Mcr-RED1-Silent


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 Mcr-RED1-Silent within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl1445 b:29.3 occ:1.00 O E:HOH2288 3.1 26.2 1.0 O E:HOH2104 3.1 31.5 1.0 O E:HOH2244 3.1 21.1 1.0 NH2 E:ARG235 3.2 24.7 1.0 CB E:ALA300 3.7 21.1 1.0 CD E:ARG235 3.8 23.8 1.0 CB E:ARG235 4.0 21.6 1.0 CG E:ARG235 4.0 22.4 1.0 CZ E:ARG235 4.2 25.8 1.0 O F:LEU248 4.4 40.0 0.0 NE E:ARG235 4.5 23.8 1.0 CB F:LEU248 4.5 39.9 1.0 CD1 F:LEU248 4.7 40.1 1.0 O E:HOH2242 4.7 21.6 1.0 O E:ALA232 4.7 20.2 1.0 O E:HOH2286 4.8 56.0 1.0 OD1 E:ASP298 4.8 26.1 1.0 N E:MET236 4.9 21.0 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