Zinc in PDB 4ay7: Methyltransferase From Methanosarcina Mazei

All present enzymatic activity of Methyltransferase From Methanosarcina Mazei:
2.1.1.247;

The structure of Methyltransferase From Methanosarcina Mazei, PDB code: 4ay7 was solved by A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	83.71 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.209, 167.419, 45.849, 90.00, 117.36, 90.00
R / Rfree (%)	16.304 / 21.287

The structure of Methyltransferase From Methanosarcina Mazei also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Methyltransferase From Methanosarcina Mazei (pdb code 4ay7). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Methyltransferase From Methanosarcina Mazei, PDB code: 4ay7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Methyltransferase From Methanosarcina Mazei


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Methyltransferase From Methanosarcina Mazei within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn500 b:46.9 occ:1.00 NE2 A:HIS240 2.2 24.5 1.0 SG A:CYS242 2.4 39.5 1.0 SG A:CYS319 2.5 40.5 1.0 CB A:CYS242 2.8 31.8 1.0 CE1 A:HIS240 3.1 21.6 1.0 CA A:CYS242 3.2 28.5 1.0 CD2 A:HIS240 3.3 23.1 1.0 CB A:CYS319 3.6 30.7 1.0 N A:CYS242 3.8 24.8 1.0 O A:HOH2202 3.9 43.2 1.0 CA A:CYS319 4.2 27.4 1.0 CG A:GLU263 4.2 39.8 1.0 CD A:GLU263 4.2 45.4 1.0 OE1 A:GLU263 4.3 40.9 1.0 ND1 A:HIS240 4.3 20.5 1.0 CG A:HIS240 4.4 20.5 1.0 C A:CYS242 4.5 27.8 1.0 O A:GLY318 4.6 25.8 1.0 C A:ILE241 4.7 22.5 1.0 OE2 A:GLU263 4.7 54.8 1.0 N A:GLY243 4.9 28.3 1.0

Zinc binding site 2 out of 2 in the Methyltransferase From Methanosarcina Mazei


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Methyltransferase From Methanosarcina Mazei within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn500 b:50.4 occ:1.00 NE2 B:HIS240 2.2 23.4 1.0 SG B:CYS319 2.3 32.3 1.0 OE2 B:GLU263 2.5 44.6 1.0 SG B:CYS242 2.6 46.2 1.0 CE1 B:HIS240 3.1 23.4 1.0 CB B:CYS242 3.2 35.1 1.0 CD2 B:HIS240 3.3 22.9 1.0 CA B:CYS242 3.4 32.3 1.0 CB B:CYS319 3.4 30.1 1.0 CD B:GLU263 3.6 46.9 1.0 CG B:GLU263 3.9 40.6 1.0 N B:CYS242 4.0 27.9 1.0 CA B:CYS319 4.1 28.1 1.0 ND1 B:HIS240 4.3 22.2 1.0 CG B:HIS240 4.4 20.7 1.0 O B:GLY318 4.6 31.1 1.0 OE1 B:GLU263 4.7 48.1 1.0 C B:CYS242 4.7 31.6 1.0 C B:ILE241 4.7 26.0 1.0 N B:GLY243 4.8 32.6 1.0 O B:ILE241 4.9 26.6 1.0

A.Hoeppner, F.Thomas, A.Rueppel, R.Hensel, W.Blankenfeldt, P.Bayer, A.Faust. Structure of the Corrinoid:Coenzyme M Methyltransferase Mtaa From Methanosarcina Mazei Acta Crystallogr.,Sect.D V. 68 1549 2012.
ISSN: ISSN 0907-4449
PubMed: 23090404
DOI: 10.1107/S090744491203853X