Chlorine in PDB 1hbu: Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M

The structure of Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M, PDB code: 1hbu 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 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	81.100, 116.500, 121.800, 90.00, 91.80, 90.00
R / Rfree (%)	16.2 / 21.1

The structure of Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M also contains other interesting chemical elements:

Nickel	(Ni)	2 atoms
Magnesium	(Mg)	13 atoms
Zinc	(Zn)	1 atom
Sodium	(Na)	9 atoms

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

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


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 in the Mcr-RED1-Silent State in Complex with Coenzyme M within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1446 b:27.9 occ:1.00 O B:HOH2116 3.0 24.6 1.0 O B:HOH2254 3.1 16.4 1.0 O B:HOH2321 3.1 19.4 1.0 NH2 B:ARG235 3.2 13.6 1.0 CD B:ARG235 3.7 13.9 1.0 CB B:ALA300 3.7 16.7 1.0 CB B:ARG235 3.9 12.8 1.0 CG B:ARG235 4.0 13.9 1.0 CD1 C:LEU248 4.0 50.4 1.0 CZ B:ARG235 4.2 14.5 1.0 NE B:ARG235 4.4 14.3 1.0 O C:LEU248 4.5 50.5 1.0 O B:HOH2252 4.7 16.9 1.0 O B:ALA232 4.7 18.1 1.0 CB C:LEU248 4.7 49.1 1.0 O B:HOH2256 4.7 46.7 1.0 OD1 B:ASP298 4.8 16.9 1.0 N B:MET236 4.8 12.5 1.0 O B:HOH2257 4.9 68.2 1.0 CG C:LEU248 5.0 49.2 1.0

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


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 in the Mcr-RED1-Silent State in Complex with Coenzyme M within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl1445 b:29.6 occ:1.00 O E:HOH2104 3.1 38.5 1.0 O E:HOH2301 3.1 20.3 1.0 O E:HOH2245 3.1 16.6 1.0 NH2 E:ARG235 3.2 21.5 1.0 CB E:ALA300 3.7 17.8 1.0 CD E:ARG235 3.8 19.0 1.0 CG E:ARG235 3.9 17.9 1.0 CB E:ARG235 3.9 18.6 1.0 CD1 F:LEU248 4.0 49.6 1.0 CZ E:ARG235 4.3 23.2 1.0 NE E:ARG235 4.5 21.4 1.0 CB F:LEU248 4.6 48.7 1.0 O E:HOH2248 4.7 20.5 1.0 O E:ALA232 4.7 20.7 1.0 OD1 E:ASP298 4.8 22.4 1.0 O F:LEU248 4.8 43.2 0.0 O E:HOH2249 4.8 49.2 1.0 N E:MET236 4.8 18.7 1.0 CG F:LEU248 4.9 49.1 1.0 CA E:ARG235 5.0 18.4 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