Magnesium in PDB 6z2a: Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah

All present enzymatic activity of Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah:
2.1.1.355;

The structure of Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah, PDB code: 6z2a was solved by A.Stirpe, T.Schalch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.68 / 2.46
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.444, 110.288, 70.684, 90, 90, 90
R / Rfree (%)	23.9 / 25

The structure of Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah also contains other interesting chemical elements:

Zinc

(Zn)

8 atoms

The binding sites of Magnesium atom in the Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah (pdb code 6z2a). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah, PDB code: 6z2a:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg506 b:30.4 occ:1.00 O A:GLY453 1.7 35.9 1.0 OD1 A:ASP386 2.8 36.5 1.0 OD2 A:ASP386 2.8 38.9 1.0 C A:GLY453 3.0 34.4 1.0 CG A:ASP386 3.1 37.6 1.0 CA A:GLY453 3.9 35.0 1.0 N A:ALA454 3.9 34.0 1.0 CA A:ALA454 4.1 33.1 1.0 O A:ALA454 4.6 35.3 1.0 CB A:ASP386 4.7 38.3 1.0 CB A:ASP384 4.7 33.4 1.0 O A:ASP384 4.8 28.7 1.0 C A:ALA454 4.9 34.2 1.0

Magnesium binding site 2 out of 2 in the Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of CLR4 Mutant - F256A/F310A/F427A Bound to Sah within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg506 b:31.9 occ:1.00 OE2 B:GLU360 3.1 22.4 1.0 NE B:ARG244 3.4 20.4 1.0 CE1 B:TYR401 3.8 20.9 1.0 CG B:ARG244 3.9 18.9 1.0 NH2 B:ARG244 4.0 22.7 1.0 CD B:GLU360 4.0 21.1 1.0 OH B:TYR401 4.1 22.9 1.0 CZ B:ARG244 4.1 21.5 1.0 CZ B:TYR401 4.2 21.5 1.0 CD B:ARG244 4.3 19.5 1.0 CG B:GLU360 4.3 19.9 1.0 CD1 B:TYR401 4.5 19.7 1.0 CG2 B:THR246 4.5 23.1 1.0 O B:LEU245 4.9 22.7 1.0

A.Stirpe, N.Guidotti, S.Northall, S.Kilic, A.Hainard, O.Vadas, B.Fierz, T.Schalch. Heterochromatin Depends on Sensing of Histone H3K14 Ubiquitination By the Set Domain of CLR4SUV39 To Be Published.