Atomistry » Magnesium » PDB 4fi3-4frz » 4fmo
Atomistry »
  Magnesium »
    PDB 4fi3-4frz »
      4fmo »

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

Protein crystallography data

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

Other elements in 4fmo:

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

Magnesium Binding Sites:

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 4fmo

Go back to Magnesium Binding Sites List in 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

Reference:

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
Page generated: Mon Dec 14 15:33:37 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy