Zinc 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
Chlorine	(Cl)	2 atoms
Sodium	(Na)	10 atoms

The binding sites of Zinc atom in the Methyl-Coenzyme M Reductase (pdb code 1hbn). 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, PDB code: 1hbn:

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


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 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1557 b:14.9 occ:0.50 O A:CYS218 2.7 11.4 1.0 O D:CYS218 2.7 11.0 1.0 O A:ARG216 2.8 11.5 1.0 O D:ARG216 2.8 11.5 1.0 O A:SER215 3.3 11.6 1.0 O D:SER215 3.3 11.9 1.0 NH2 D:ARG102 3.5 12.5 1.0 NH2 A:ARG102 3.5 12.5 1.0 C D:ARG216 3.6 10.6 1.0 C A:ARG216 3.6 9.8 1.0 C A:CYS218 3.8 10.7 1.0 C D:CYS218 3.8 10.2 1.0 O D:HOH2321 3.9 14.1 1.0 CA D:ARG216 3.9 10.2 1.0 CA A:ARG216 3.9 10.4 1.0 O A:HOH2309 3.9 14.4 1.0 CZ D:ARG102 4.0 12.2 1.0 CZ A:ARG102 4.1 12.3 1.0 NH1 A:ARG102 4.1 12.6 1.0 NH1 D:ARG102 4.1 13.0 1.0 C D:SER215 4.3 10.6 1.0 C A:SER215 4.3 10.9 1.0 N D:CYS218 4.3 10.5 1.0 N A:CYS218 4.4 10.4 1.0 C A:THR217 4.5 10.2 1.0 CA A:ASP219 4.6 11.0 1.0 C D:THR217 4.6 10.1 1.0 N D:ARG216 4.6 10.3 1.0 N D:ASP219 4.6 10.7 1.0 N A:ARG216 4.6 9.9 1.0 N A:ASP219 4.6 11.1 1.0 CA D:ASP219 4.6 10.8 1.0 N D:THR217 4.6 10.7 1.0 N A:THR217 4.6 9.9 1.0 CA A:CYS218 4.7 10.6 1.0 CA D:CYS218 4.7 10.6 1.0 O A:THR217 4.9 11.3 1.0 O D:THR217 4.9 11.2 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