Magnesium in PDB 4fmo: Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1

The structure of Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1, PDB code: 4fmo was solved by E.Gueneau, P.Legrand, J.B.Charbonnier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.41 / 3.04
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	193.700, 66.140, 74.470, 90.00, 91.28, 90.00
R / Rfree (%)	18 / 19.6

The structure of Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Magnesium atom in the Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1 (pdb code 4fmo). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1, PDB code: 4fmo:

Magnesium binding site 1 out of 1 in the Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the C-Terminal Domain of the Saccharomyces Cerevisiae Mutl Alpha (MLH1/PMS1) Heterodimer Bound to A Fragment of EXO1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg801 b:46.6 occ:1.00 NE2 A:HIS553 2.2 95.1 1.0 OD2 A:ASP531 2.4 0.5 1.0 CE1 A:HIS553 2.7 95.6 1.0 CG A:ASP531 3.1 1.0 1.0 OD1 A:ASP531 3.2 0.7 1.0 O A:HOH914 3.4 88.1 1.0 CD2 A:HIS553 3.5 93.2 1.0 OD1 A:ASP554 3.8 0.4 1.0 ND1 A:HIS553 4.0 95.1 1.0 O A:ASP531 4.2 79.8 1.0 OD2 A:ASP554 4.3 0.4 1.0 CB A:ASN535 4.3 84.2 1.0 OD1 A:ASN535 4.3 0.9 1.0 CG A:ASP554 4.3 0.8 1.0 CG A:HIS553 4.4 91.1 1.0 CG A:ASN535 4.5 0.8 1.0 CB A:ASP531 4.5 83.5 1.0 C A:ASP531 4.5 79.7 1.0 N A:ILE532 5.0 74.1 1.0

E.Gueneau, C.Dherin, P.Legrand, C.Tellier-Lebegue, B.Gilquin, P.Bonnesoeur, F.Londino, C.Quemener, M.H.Le Du, J.A.Marquez, M.Moutiez, M.Gondry, S.Boiteux, J.B.Charbonnier. Structure of the Mutl Alpha C-Terminal Domain Reveals How MLH1 Contributes to PMS1 Endonuclease Site. Nat.Struct.Mol.Biol. V. 20 461 2013.
ISSN: ISSN 1545-9993
PubMed: 23435383
DOI: 10.1038/NSMB.2511