Zinc 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
Chlorine	(Cl)	2 atoms
Sodium	(Na)	9 atoms

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Methyl-Coenzyme M Reductase in the Mcr-RED1-Silent State in Complex with Coenzyme M, PDB code: 1hbu:

Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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 A:Zn1557 b:17.0 occ:0.50 O D:CYS218 2.8 11.8 1.0 O A:CYS218 2.8 14.3 1.0 O A:ARG216 2.8 12.8 1.0 O D:ARG216 2.8 14.1 1.0 O A:SER215 3.3 12.1 1.0 NH2 A:ARG102 3.4 11.8 1.0 O D:SER215 3.4 12.8 1.0 NH2 D:ARG102 3.5 7.5 1.0 C A:ARG216 3.6 12.7 1.0 C D:ARG216 3.6 13.9 1.0 O A:HOH2269 3.8 11.6 1.0 O D:HOH2274 3.8 9.9 1.0 C A:CYS218 3.8 14.2 1.0 CA A:ARG216 3.8 12.7 1.0 CA D:ARG216 3.9 13.2 1.0 C D:CYS218 3.9 10.9 1.0 CZ A:ARG102 3.9 13.3 1.0 NH1 D:ARG102 4.0 10.4 1.0 CZ D:ARG102 4.0 9.9 1.0 NH1 A:ARG102 4.0 12.8 1.0 N A:CYS218 4.3 11.1 1.0 C D:SER215 4.4 12.9 1.0 C A:SER215 4.4 13.7 1.0 N D:CYS218 4.4 10.0 1.0 C A:THR217 4.5 10.9 1.0 C D:THR217 4.5 11.0 1.0 CA A:ASP219 4.6 13.1 1.0 N D:ARG216 4.6 12.0 1.0 N A:ARG216 4.6 14.1 1.0 CA D:ASP219 4.6 11.5 1.0 N A:ASP219 4.6 14.8 1.0 N D:ASP219 4.7 10.5 1.0 N D:THR217 4.7 11.5 1.0 N A:THR217 4.7 10.8 1.0 CA A:CYS218 4.7 11.0 1.0 CA D:CYS218 4.7 11.2 1.0 O D:THR217 4.8 12.6 1.0 O A:THR217 4.8 10.6 1.0 NE A:ARG102 4.9 12.6 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