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Sodium in PDB 6bkg: Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation

Enzymatic activity of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation

All present enzymatic activity of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation:
6.5.1.1;

Protein crystallography data

The structure of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation, PDB code: 6bkg was solved by A.F.Moon, P.P.Tumbale, M.J.Schellenberg, R.S.Williams, J.G.Williams, T.A.Kunkel, L.C.Pedersen, B.Bebenek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.20 / 2.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 72.657, 102.747, 110.131, 90.00, 90.00, 90.00
R / Rfree (%) 20.1 / 24.5

Other elements in 6bkg:

The structure of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation (pdb code 6bkg). 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 Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation, PDB code: 6bkg:

Sodium binding site 1 out of 1 in 6bkg

Go back to Sodium Binding Sites List in 6bkg
Sodium binding site 1 out of 1 in the Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human Ligiv Catalytic Domain with Bound Dna-Adenylate Intermediate in Closed Conformation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na703

b:52.7
occ:1.00
O A:GLY509 2.4 33.5 1.0
O A:HOH808 2.4 36.7 1.0
OP1 D:DG5 2.4 38.6 1.0
O A:HOH801 2.4 21.1 0.8
O A:HOH864 2.5 39.6 0.9
C A:GLY509 3.4 32.5 1.0
O A:ILE581 3.7 26.2 1.0
P D:DG5 3.7 34.9 1.0
CA A:GLY509 3.8 22.0 1.0
O3' D:DC4 3.9 36.8 1.0
O A:GLU582 4.1 27.9 1.0
N A:CYS510 4.6 30.8 1.0
OP2 D:DG5 4.7 37.6 1.0
O5' D:DG5 4.7 28.0 1.0
CA A:GLU582 4.8 29.8 1.0
C5' D:DG5 4.8 29.8 1.0
C A:GLU582 4.8 26.5 1.0
C A:ILE581 4.8 23.8 1.0

Reference:

A.M.Kaminski, P.P.Tumbale, M.J.Schellenberg, R.S.Williams, J.G.Williams, T.A.Kunkel, L.C.Pedersen, K.Bebenek. Structures of Dna-Bound Human Ligase IV Catalytic Core Reveal Insights Into Substrate Binding and Catalysis. Nat Commun V. 9 2642 2018.
ISSN: ESSN 2041-1723
PubMed: 29980672
DOI: 10.1038/S41467-018-05024-8
Page generated: Tue Oct 8 02:11:44 2024

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