Magnesium in PDB 9f6d: Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation)

All present enzymatic activity of Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation):
2.7.7.7;

The structure of Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation) also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Magnesium atom in the Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation) (pdb code 9f6d). 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 Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation), PDB code: 9f6d:

Magnesium binding site 1 out of 1 in the Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Dna Polymerase Epsilon Bound to Dna and Pcna (Open Conformation) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1303 b:18.4 occ:1.00 O1A A:DDS1302 2.1 25.3 1.0 OD2 A:ASP862 2.1 15.6 1.0 O2B A:DDS1302 2.5 25.3 1.0 O A:VAL627 2.5 11.6 1.0 O3G A:DDS1302 2.6 25.3 1.0 PA A:DDS1302 3.2 25.3 1.0 CG A:ASP862 3.3 15.6 1.0 PB A:DDS1302 3.4 25.3 1.0 O3B A:DDS1302 3.5 25.3 1.0 O3A A:DDS1302 3.6 25.3 1.0 PG A:DDS1302 3.6 25.3 1.0 O5' A:DDS1302 3.7 25.3 1.0 C A:VAL627 3.7 11.6 1.0 OD1 A:ASP862 4.1 15.6 1.0 N A:ALA629 4.2 17.0 1.0 CB A:ASP862 4.3 15.6 1.0 CA A:GLY628 4.4 15.2 1.0 OD2 A:ASP626 4.4 16.6 1.0 N A:GLY628 4.5 15.2 1.0 O2G A:DDS1302 4.5 25.3 1.0 O2A A:DDS1302 4.6 25.3 1.0 N A:VAL627 4.7 11.6 1.0 C5' A:DDS1302 4.7 25.3 1.0 C A:GLY628 4.7 15.2 1.0 CG A:ASP626 4.7 16.6 1.0 CA A:VAL627 4.7 11.6 1.0 O1G A:DDS1302 4.8 25.3 1.0 O1B A:DDS1302 4.8 25.3 1.0 N A:MET630 4.8 16.4 1.0

J.J.Roske, J.T.P.Yeeles. Structural Basis For Processive Daughter-Strand Synthesis and Proofreading By the Human Leading-Strand Dna Polymerase Pol Epsilon. Nat.Struct.Mol.Biol. 2024.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-024-01370-Y