Bromine in PDB 2qc6: Protein Kinase CK2 in Complex with Dbc

All present enzymatic activity of Protein Kinase CK2 in Complex with Dbc:
2.7.11.1;

The structure of Protein Kinase CK2 in Complex with Dbc, PDB code: 2qc6 was solved by R.Battistutta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.85
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	141.676, 60.252, 44.901, 90.00, 103.00, 90.00
R / Rfree (%)	21.4 / 26.8

The binding sites of Bromine atom in the Protein Kinase CK2 in Complex with Dbc (pdb code 2qc6). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 2 binding sites of Bromine where determined in the Protein Kinase CK2 in Complex with Dbc, PDB code: 2qc6:
Jump to Bromine binding site number: 1; 2;

Bromine binding site 1 out of 2 in the Protein Kinase CK2 in Complex with Dbc


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Protein Kinase CK2 in Complex with Dbc within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1 b:52.0 occ:1.00 BR2 A:G121 0.0 52.0 1.0 C9 A:G121 1.9 45.0 1.0 C10 A:G121 2.9 44.2 1.0 C8 A:G121 3.0 44.7 1.0 C13 A:G121 3.2 44.6 1.0 O15 A:G121 3.2 44.6 1.0 SD A:MET163 3.6 25.6 1.0 O A:HOH452 3.6 32.8 1.0 O A:VAL116 3.7 32.4 1.0 CD1 A:ILE66 3.7 27.6 1.0 CG A:MET163 4.0 25.0 1.0 CG1 A:ILE66 4.2 25.7 1.0 O7 A:G121 4.2 45.0 1.0 C5 A:G121 4.3 45.1 1.0 CG2 A:VAL45 4.5 30.1 1.0 O A:HOH441 4.6 34.4 1.0 CB A:ASN118 4.7 34.4 1.0 C A:VAL116 4.7 32.0 1.0 CB A:VAL116 4.7 30.9 1.0 C6 A:G121 4.7 45.4 1.0 CB A:MET163 4.9 24.4 1.0

Bromine binding site 2 out of 2 in the Protein Kinase CK2 in Complex with Dbc


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Protein Kinase CK2 in Complex with Dbc within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1 b:44.8 occ:1.00 BR1 A:G121 0.0 44.8 1.0 C4 A:G121 1.9 45.4 1.0 C6 A:G121 2.8 45.4 1.0 C3 A:G121 2.9 44.7 1.0 O7 A:G121 2.9 45.0 1.0 O11 A:G121 3.1 44.4 1.0 NZ A:LYS68 3.6 18.8 1.0 CB A:ASP175 3.7 21.4 1.0 CE A:LYS68 3.8 22.7 1.0 CG A:ASP175 3.9 22.5 1.0 CG2 A:VAL53 3.9 22.4 1.0 O A:HOH344 4.0 14.6 1.0 CD A:LYS68 4.0 23.4 1.0 OD2 A:ASP175 4.0 26.1 1.0 C5 A:G121 4.1 45.1 1.0 C2 A:G121 4.2 45.3 1.0 CD1 A:ILE174 4.2 18.4 1.0 O A:HOH519 4.2 37.1 1.0 CA A:ASP175 4.2 20.7 1.0 C8 A:G121 4.3 44.7 1.0 OG A:SER51 4.3 20.7 1.0 O A:HOH533 4.4 24.3 1.0 N A:ASP175 4.4 20.4 1.0 OD1 A:ASP175 4.4 25.7 1.0 CG A:LYS68 4.5 22.5 1.0 O A:HOH449 4.5 25.7 1.0 C1 A:G121 4.7 45.0 1.0 O15 A:G121 4.8 44.6 1.0 O A:HOH405 4.9 22.9 1.0 O A:HOH418 4.9 20.4 1.0

A.Chilin, R.Battistutta, A.Bortolato, G.Cozza, S.Zanatta, G.Poletto, M.Mazzorana, G.Zagotto, E.Uriarte, A.Guiotto, L.A.Pinna, F.Meggio, S.Moro. Coumarin As Attractive Casein Kinase 2 (CK2) Inhibitor Scaffold: An Integrate Approach to Elucidate the Putative Binding Motif and Explain Structure-Activity Relationships. J.Med.Chem. V. 51 752 2008.
ISSN: ISSN 0022-2623
PubMed: 18251491
DOI: 10.1021/JM070909T