Chlorine in PDB 3nga: Human CK2 Catalytic Domain in Complex with Cx-4945

All present enzymatic activity of Human CK2 Catalytic Domain in Complex with Cx-4945:
2.7.11.1;

The structure of Human CK2 Catalytic Domain in Complex with Cx-4945, PDB code: 3nga was solved by A.D.Ferguson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.67 / 2.71
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	127.640, 127.640, 125.750, 90.00, 90.00, 90.00
R / Rfree (%)	18.8 / 21.8

The binding sites of Chlorine atom in the Human CK2 Catalytic Domain in Complex with Cx-4945 (pdb code 3nga). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human CK2 Catalytic Domain in Complex with Cx-4945, PDB code: 3nga:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human CK2 Catalytic Domain in Complex with Cx-4945


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human CK2 Catalytic Domain in Complex with Cx-4945 within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1000 b:78.6 occ:1.00 CL22 A:3NG1000 0.0 78.6 1.0 C18 A:3NG1000 1.7 59.6 1.0 C19 A:3NG1000 2.7 52.2 1.0 C17 A:3NG1000 2.7 49.2 1.0 C A:GLY46 3.3 47.9 1.0 CA A:GLY46 3.5 40.2 1.0 O A:GLY46 3.6 46.2 1.0 N A:ARG47 3.8 51.6 1.0 CB A:VAL53 3.8 43.5 1.0 CG2 A:VAL53 3.8 41.9 1.0 C20 A:3NG1000 4.0 51.3 1.0 C16 A:3NG1000 4.0 46.0 1.0 N A:GLY46 4.0 39.8 1.0 C A:ARG47 4.3 62.4 1.0 O A:ARG47 4.4 61.8 1.0 CA A:ARG47 4.5 54.1 1.0 C21 A:3NG1000 4.5 47.6 1.0 O A:HOH384 4.6 43.3 1.0 N A:VAL53 4.7 43.1 1.0 N A:GLY48 4.7 62.8 1.0 C A:LEU45 4.7 45.3 1.0 NE2 A:HIS160 4.7 54.0 1.0 CE1 A:HIS160 4.7 53.0 1.0 CG1 A:VAL53 4.8 42.6 1.0 CA A:VAL53 4.8 40.3 1.0 O A:LEU45 4.9 48.8 1.0

Chlorine binding site 2 out of 2 in the Human CK2 Catalytic Domain in Complex with Cx-4945


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human CK2 Catalytic Domain in Complex with Cx-4945 within 5.0Å range: probe atom residue distance (Å) B Occ B:Cl1000 b:79.7 occ:1.00 CL22 B:3NG1000 0.0 79.7 1.0 C18 B:3NG1000 1.7 64.0 1.0 C17 B:3NG1000 2.7 56.1 1.0 C19 B:3NG1000 2.7 54.3 1.0 C B:GLY46 3.3 56.3 1.0 CA B:GLY46 3.4 49.1 1.0 O B:GLY46 3.6 56.1 1.0 N B:ARG47 3.7 57.3 1.0 CG2 B:VAL53 3.8 38.9 1.0 CB B:VAL53 3.8 41.1 1.0 C16 B:3NG1000 4.0 50.9 1.0 C20 B:3NG1000 4.0 51.3 1.0 N B:GLY46 4.0 48.4 1.0 O B:ARG47 4.1 67.5 1.0 C B:ARG47 4.3 66.1 1.0 N B:VAL53 4.4 44.3 1.0 C21 B:3NG1000 4.4 51.7 1.0 CA B:ARG47 4.5 59.1 1.0 CA B:VAL53 4.6 41.5 1.0 NE2 B:HIS160 4.7 57.5 1.0 C B:LEU45 4.7 49.3 1.0 O B:HOH340 4.7 46.2 1.0 CE1 B:HIS160 4.8 58.1 1.0 CG1 B:VAL53 4.9 40.7 1.0 N B:GLY48 4.9 63.4 1.0 O B:LEU45 5.0 50.7 1.0

A.D.Ferguson, P.R.Sheth, A.D.Basso, S.Paliwal, K.Gray, T.O.Fischmann, H.V.Le. Structural Basis of Cx-4945 Binding to Human Protein Kinase CK2. Febs Lett. V. 585 104 2011.
ISSN: ISSN 0014-5793
PubMed: 21093442
DOI: 10.1016/J.FEBSLET.2010.11.019