Sodium in PDB 7l35: Human Dna Ligase 1 - R771W Nicked Dna Complex

All present enzymatic activity of Human Dna Ligase 1 - R771W Nicked Dna Complex:
6.5.1.1;

The structure of Human Dna Ligase 1 - R771W Nicked Dna Complex, PDB code: 7l35 was solved by P.P.Tumbale, R.S.Williams, M.S.Schellenberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.73 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.33, 100.523, 116.088, 90, 90, 90
R / Rfree (%)	16.3 / 19.5

The binding sites of Sodium atom in the Human Dna Ligase 1 - R771W Nicked Dna Complex (pdb code 7l35). 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 Human Dna Ligase 1 - R771W Nicked Dna Complex, PDB code: 7l35:

Sodium binding site 1 out of 1 in the Human Dna Ligase 1 - R771W Nicked Dna Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Dna Ligase 1 - R771W Nicked Dna Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Na101 b:45.7 occ:1.00 O B:HOH234 2.3 52.3 1.0 O B:HOH236 2.5 48.1 1.0 O B:HOH202 2.7 37.0 1.0 O6 B:DG11 2.8 18.0 0.5 O6 B:DG11 3.0 16.9 0.5 O D:HOH262 3.0 27.0 1.0 O B:HOH209 3.2 29.9 1.0 C6 B:DG11 3.8 19.1 0.5 H42 D:DC18 3.9 22.9 1.0 N7 B:DG11 3.9 19.8 0.5 H62 D:DA17 4.0 21.7 1.0 C6 B:DG11 4.0 19.3 0.5 H61 D:DA17 4.2 21.7 1.0 N7 B:DG11 4.2 24.5 0.5 H5 B:DC10 4.2 26.6 1.0 C5 B:DG11 4.2 20.4 0.5 C5 B:DC10 4.3 22.1 1.0 N6 D:DA17 4.4 18.1 1.0 O D:HOH274 4.4 54.8 1.0 C5 B:DG11 4.5 18.4 0.5 O4 B:DT12 4.5 17.2 0.6 N4 D:DC18 4.5 19.1 1.0 H41 D:DC18 4.5 22.9 1.0 O D:HOH239 4.5 32.1 1.0 O D:HOH254 4.6 29.0 1.0 O4 B:DT12 4.6 21.1 0.5 C4 B:DC10 4.7 20.4 1.0 C6 B:DC10 4.7 23.7 1.0 H41 B:DC10 4.8 32.3 1.0 H6 B:DC10 4.9 28.5 1.0 N4 B:DC10 4.9 26.9 1.0

T.J.Jurkiw, P.P.Tumbale, M.J.Schellenberg, C.Cunningham-Rundles, R.S.Williams, P.J.O'brien. LIG1 Syndrome Mutations Remodel A Cooperative Network of Ligand Binding Interactions to Compromise Ligation Efficiency To Be Published.