Sodium in PDB 3lqc: X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain

All present enzymatic activity of X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain:
2.7.7.7;

The structure of X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain, PDB code: 3lqc was solved by M.J.Cuneo, J.M.Krahn, R.E.London, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.63 / 2.35
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	75.240, 75.240, 126.160, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 25

The binding sites of Sodium atom in the X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain (pdb code 3lqc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain, PDB code: 3lqc:

Sodium binding site 1 out of 1 in the X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of X-Ray Crystal Structure of Oxidized XRCC1 Bound to Dna Pol Beta Palm Thumb Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Na278 b:19.4 occ:1.00 O A:SER74 2.8 23.2 1.0 O A:ALA76 2.9 26.4 1.0 O A:GLY78 3.0 23.6 1.0 C A:SER74 3.9 20.2 1.0 O A:HOH208 4.0 19.7 1.0 C A:ALA76 4.0 29.8 1.0 CB A:SER74 4.1 22.9 1.0 C A:GLY78 4.2 27.6 1.0 N A:GLY78 4.3 23.3 1.0 CA A:SER74 4.5 22.4 1.0 C A:GLY77 4.5 27.1 1.0 CA A:GLY77 4.6 21.8 1.0 C A:SER75 4.7 22.0 1.0 O A:SER75 4.7 27.0 1.0 N A:GLY77 4.7 29.7 1.0 N A:ALA76 4.8 24.6 1.0 OG A:SER74 4.8 29.4 1.0 N A:SER74 4.9 19.3 1.0 N A:SER75 4.9 20.9 1.0 CB A:ALA79 4.9 18.1 1.0 CA A:GLY78 4.9 26.5 1.0

M.J.Cuneo, R.E.London. Oxidation State of the XRCC1 N-Terminal Domain Regulates Dna Polymerase Beta Binding Affinity. Proc.Natl.Acad.Sci.Usa V. 107 6805 2010.
ISSN: ISSN 0027-8424
PubMed: 20351257
DOI: 10.1073/PNAS.0914077107