Magnesium in PDB 6sqw: Mouse Dctpase in Complex with 5-Me-Dcmp

All present enzymatic activity of Mouse Dctpase in Complex with 5-Me-Dcmp:
3.6.1.12;

The structure of Mouse Dctpase in Complex with 5-Me-Dcmp, PDB code: 6sqw was solved by E.R.Scaletti, M.Claesson, H.Helleday, A.S.Jemth, P.Stenmark, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.04 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	58.516, 58.516, 140.905, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 21.5

The binding sites of Magnesium atom in the Mouse Dctpase in Complex with 5-Me-Dcmp (pdb code 6sqw). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mouse Dctpase in Complex with 5-Me-Dcmp, PDB code: 6sqw:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mouse Dctpase in Complex with 5-Me-Dcmp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mouse Dctpase in Complex with 5-Me-Dcmp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:21.4 occ:1.00 OE1 A:GLU63 2.0 19.5 1.0 OE2 A:GLU66 2.1 25.9 1.0 OE1 A:GLU95 2.1 24.2 1.0 O A:HOH350 2.1 29.1 1.0 O A:HOH328 2.1 28.4 1.0 OD2 A:ASP98 2.1 21.1 1.0 CD A:GLU63 3.1 19.5 1.0 CD A:GLU95 3.1 23.2 1.0 CG A:ASP98 3.2 21.1 1.0 CD A:GLU66 3.3 26.1 1.0 OE2 A:GLU95 3.3 25.2 1.0 OE2 A:GLU63 3.5 20.6 1.0 CB A:ASP98 3.7 20.1 1.0 OE1 A:GLU66 4.0 30.0 1.0 O A:HOH355 4.1 42.5 1.0 O D:HOH325 4.2 25.9 1.0 OD1 A:ASP98 4.3 22.0 1.0 O A:HOH316 4.3 34.2 1.0 CG A:GLU66 4.4 23.6 1.0 CG A:GLU63 4.4 17.9 1.0 CB A:GLU66 4.4 21.2 1.0 OP3 A:5CM202 4.5 33.8 1.0 CG A:GLU95 4.5 22.7 1.0 CB A:GLU63 4.7 17.2 1.0 CA A:GLU95 4.8 21.1 1.0 CA A:GLU63 4.9 16.9 1.0 CB A:GLU95 5.0 21.4 1.0

Magnesium binding site 2 out of 2 in the Mouse Dctpase in Complex with 5-Me-Dcmp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mouse Dctpase in Complex with 5-Me-Dcmp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg201 b:25.1 occ:1.00 O D:HOH339 1.9 35.3 1.0 OE1 D:GLU95 2.0 26.2 1.0 OE2 D:GLU66 2.1 29.2 1.0 O D:HOH303 2.1 28.4 1.0 OE1 D:GLU63 2.1 23.6 1.0 OD2 D:ASP98 2.1 26.5 1.0 CD D:GLU95 3.1 26.5 1.0 CD D:GLU63 3.1 22.8 1.0 CG D:ASP98 3.2 26.9 1.0 CD D:GLU66 3.3 28.6 1.0 OE2 D:GLU95 3.3 27.6 1.0 OE2 D:GLU63 3.5 24.2 1.0 CB D:ASP98 3.7 25.4 1.0 OE1 D:GLU66 4.0 33.1 1.0 O A:HOH366 4.1 31.5 1.0 OD1 D:ASP98 4.3 28.0 1.0 CG D:GLU66 4.3 25.6 1.0 CB D:GLU66 4.3 23.8 1.0 OP3 D:5CM202 4.4 33.5 1.0 CG D:GLU95 4.5 26.1 1.0 CG D:GLU63 4.5 21.5 1.0 CA D:GLU95 4.8 25.8 1.0 CB D:GLU63 4.8 20.3 1.0 CA D:GLU63 4.9 19.5 1.0 CB D:GLU95 5.0 25.2 1.0

E.Scaletti, M.Claesson, T.Helleday, A.S.Jemth, P.Stenmark. The First Structure of An Active Mammalian Dctpase and Its Complexes with Substrate Analogues and Products. J.Mol.Biol. 2020.
ISSN: ESSN 1089-8638
PubMed: 31954130
DOI: 10.1016/J.JMB.2020.01.005