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Sodium in PDB 6tlv: Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole

Enzymatic activity of Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole

All present enzymatic activity of Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole:
2.7.11.1;

Protein crystallography data

The structure of Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole, PDB code: 6tlv was solved by H.Czapinska, A.Piasecka, M.Winiewska-Szajewska, M.Bochtler, J.Poznanski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.47 / 1.67
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 128.782, 128.782, 60.910, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 17.3

Other elements in 6tlv:

The structure of Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole also contains other interesting chemical elements:

Bromine (Br) 3 atoms
Chlorine (Cl) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole (pdb code 6tlv). 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 CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole, PDB code: 6tlv:

Sodium binding site 1 out of 1 in 6tlv

Go back to Sodium Binding Sites List in 6tlv
Sodium binding site 1 out of 1 in the Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Human CK2 Kinase Alpha Subunit in Complex with the Atp-Competitive Inhibitor 5-Bromobenzotriazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na406

b:54.3
occ:1.00
 O A:HOH889 2.2 51.5 1.0
O A:GLN290 2.2 36.7 0.5
O A:VAL293 2.3 34.4 1.0
O A:GLN290 2.3 37.0 0.5
O A:HOH655 2.4 70.7 1.0
O A:HOH784 2.5 51.4 1.0
O A:HOH938 2.7 50.3 1.0
C A:GLN290 3.5 35.6 0.5
C A:GLN290 3.5 36.2 0.5
C A:VAL293 3.5 31.7 1.0
O A:HOH1008 3.6 48.7 1.0
OE1 A:GLN290 4.1 45.4 0.5
CA A:GLN290 4.3 36.3 0.5
CA A:GLN290 4.3 35.3 0.5
O A:HOH848 4.3 46.6 1.0
N A:VAL293 4.3 31.1 1.0
CA A:VAL293 4.3 30.0 1.0
O A:HOH1002 4.3 62.3 1.0
O A:HOH963 4.4 44.6 1.0
N A:HIS291 4.4 35.8 1.0
N A:SER294 4.4 29.2 1.0
CB A:GLN290 4.5 39.1 0.5
CB A:GLN290 4.5 37.1 0.5
CB A:VAL293 4.6 31.2 1.0
O A:HOH1095 4.6 57.6 1.0
CA A:HIS291 4.6 36.2 1.0
CA A:SER294 4.6 29.1 1.0
O A:HOH507 4.8 65.8 1.0
C A:HIS291 4.8 34.7 1.0

Reference:

H.Czapinska, A.Piasecka, M.Winiewska-Szajewska, M.Bochtler, J.Poznanski. Binding of Bromobenzotriazoles By the Catalytic Subunit of Human Protein Kinase CK2: Structural and Thermodynamics Studies. To Be Published.
Page generated: Tue Oct 8 13:59:35 2024

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