Magnesium in PDB 6ipl: Binary Complex of Human Dna Polymerase Mu with Mgdatp

All present enzymatic activity of Binary Complex of Human Dna Polymerase Mu with Mgdatp:
2.7.7.7;

The structure of Binary Complex of Human Dna Polymerase Mu with Mgdatp, PDB code: 6ipl was solved by Y.K.Chang, W.J.Wu, M.D.Tsai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.64
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	124.879, 124.879, 50.561, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 24

The binding sites of Magnesium atom in the Binary Complex of Human Dna Polymerase Mu with Mgdatp (pdb code 6ipl). 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 Binary Complex of Human Dna Polymerase Mu with Mgdatp, PDB code: 6ipl:

Magnesium binding site 1 out of 1 in the Binary Complex of Human Dna Polymerase Mu with Mgdatp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Binary Complex of Human Dna Polymerase Mu with Mgdatp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:22.9 occ:1.00 O1B A:DTP502 1.8 18.2 0.5 O1A A:DTP502 2.0 22.5 0.5 O1A A:DTP502 2.0 20.3 0.5 OD1 A:ASP330 2.1 11.4 1.0 O A:HOH697 2.1 9.5 1.0 OD2 A:ASP332 2.2 7.4 0.5 O2G A:DTP502 2.3 18.9 0.5 O1B A:DTP502 2.3 22.2 0.5 PB A:DTP502 3.1 19.1 0.5 O A:HOH602 3.1 30.0 0.5 OD2 A:ASP332 3.1 7.3 0.5 PB A:DTP502 3.2 23.2 0.5 CG A:ASP332 3.2 7.5 0.5 CG A:ASP330 3.2 10.8 1.0 PA A:DTP502 3.3 21.3 0.5 PA A:DTP502 3.3 23.6 0.5 PG A:DTP502 3.6 18.1 0.5 O3A A:DTP502 3.6 20.1 0.5 OD1 A:ASP332 3.6 7.5 0.5 O2B A:DTP502 3.6 22.9 0.5 O3A A:DTP502 3.6 23.3 0.5 OD2 A:ASP330 3.7 11.2 1.0 O3B A:DTP502 3.8 18.8 0.5 CG A:ASP332 3.8 7.4 0.5 O A:ASP330 3.8 8.6 1.0 O A:HOH775 4.0 8.3 1.0 C A:ASP330 4.1 8.8 1.0 ND1 A:HIS329 4.2 10.9 0.5 OD1 A:ASP332 4.2 7.3 0.5 C5' A:DTP502 4.2 25.2 0.5 C5' A:DTP502 4.2 23.6 0.5 N A:GLY320 4.2 8.3 1.0 CE1 A:HIS329 4.2 11.1 0.5 O5' A:DTP502 4.3 22.4 0.5 O5' A:DTP502 4.3 24.4 0.5 O2A A:DTP502 4.4 23.2 0.5 CA A:GLY319 4.4 8.1 1.0 O2A A:DTP502 4.4 20.9 0.5 O2B A:DTP502 4.4 19.1 0.5 O1G A:DTP502 4.4 18.8 0.5 CB A:ASP330 4.5 10.2 1.0 CB A:ASP332 4.5 7.6 0.5 O A:HOH617 4.6 16.0 1.0 N A:ASP330 4.6 9.9 1.0 CA A:ASP330 4.6 9.6 1.0 CB A:ASP332 4.6 7.5 0.5 O3G A:DTP502 4.6 19.2 0.5 N A:VAL331 4.7 8.1 1.0 N A:ASP332 4.7 7.5 0.5 O3B A:DTP502 4.7 23.2 0.5 CE1 A:HIS329 4.7 12.9 0.5 N A:ASP332 4.7 7.5 0.5 C A:GLY319 4.9 8.2 1.0 O A:HOH766 4.9 16.2 1.0 CA A:VAL331 4.9 7.8 1.0 C A:VAL331 5.0 7.5 1.0

Y.K.Chang, Y.P.Huang, X.X.Liu, T.P.Ko, Y.Bessho, Y.Kawano, M.Maestre-Reyna, W.J.Wu, M.D.Tsai. Human Dna Polymerase Mu Can Use A Noncanonical Mechanism For Multiple MN2+-Mediated Functions. J.Am.Chem.Soc. V. 141 8489 2019.
ISSN: ESSN 1520-5126
PubMed: 31067051
DOI: 10.1021/JACS.9B01741