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Bromine in PDB 4kwp: Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution

Enzymatic activity of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution

All present enzymatic activity of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution:
2.7.11.1;

Protein crystallography data

The structure of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution, PDB code: 4kwp was solved by A.Ranchio, G.Lolli, R.Battistutta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.24 / 1.25
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.448, 45.821, 63.486, 90.00, 111.15, 90.00
R / Rfree (%) 13.6 / 17

Bromine Binding Sites:

The binding sites of Bromine atom in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution (pdb code 4kwp). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution, PDB code: 4kwp:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in 4kwp

Go back to Bromine Binding Sites List in 4kwp
Bromine binding site 1 out of 4 in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br408

b:22.9
occ:1.00
 BRE A:EXX408 0.0 22.9 1.0
CAN A:EXX408 1.9 15.4 1.0
CAP A:EXX408 2.8 18.6 1.0
CAL A:EXX408 2.9 18.6 1.0
HE3 A:LYS68 2.9 22.1 1.0
HD2 A:LYS68 3.0 19.1 1.0
HD12 A:ILE174 3.1 14.7 1.0
NAJ A:EXX408 3.2 22.8 1.0
O A:HOH576 3.3 19.4 1.0
HG11 A:VAL53 3.4 20.8 1.0
BRC A:EXX408 3.4 28.4 1.0
O A:HOH744 3.4 34.9 1.0
OD1 A:ASP175 3.5 17.3 1.0
CE A:LYS68 3.6 18.5 1.0
HG21 A:VAL53 3.7 21.4 1.0
CD A:LYS68 3.7 15.9 1.0
HZ2 A:LYS68 3.7 24.9 1.0
CD1 A:ILE174 3.8 12.3 1.0
HG11 A:VAL66 3.8 17.2 1.0
HD13 A:ILE174 3.8 14.7 1.0
HG13 A:VAL53 3.8 20.8 1.0
HG2 A:LYS68 3.9 18.7 1.0
CG1 A:VAL53 4.1 17.3 1.0
HD11 A:ILE174 4.1 14.7 1.0
HG22 A:VAL53 4.1 21.4 1.0
CAM A:EXX408 4.1 18.8 1.0
OD2 A:ASP175 4.1 15.7 1.0
CAQ A:EXX408 4.1 19.9 1.0
CG A:ASP175 4.2 15.6 1.0
NZ A:LYS68 4.2 20.8 1.0
O A:HOH822 4.2 11.3 1.0
CG A:LYS68 4.2 15.6 1.0
CG2 A:VAL53 4.3 17.9 1.0
HG3 A:LYS68 4.4 18.7 1.0
HE2 A:LYS68 4.4 22.1 1.0
HE3 A:MET163 4.5 15.0 0.5
HD3 A:LYS68 4.5 19.1 1.0
HZ1 A:LYS68 4.5 24.9 1.0
HG12 A:VAL66 4.5 17.2 1.0
CAG A:EXX408 4.6 24.3 1.0
CG1 A:VAL66 4.6 14.3 1.0
CAO A:EXX408 4.6 18.1 1.0
HB A:ILE174 4.7 11.3 1.0
HG12 A:VAL53 4.8 20.8 1.0
CB A:VAL53 4.8 15.5 1.0
HZ3 A:LYS68 4.9 24.9 1.0
HG13 A:VAL66 5.0 17.2 1.0

Bromine binding site 2 out of 4 in 4kwp

Go back to Bromine Binding Sites List in 4kwp
Bromine binding site 2 out of 4 in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br408

b:28.4
occ:1.00
 BRC A:EXX408 0.0 28.4 1.0
CAL A:EXX408 2.0 18.6 1.0
CAM A:EXX408 2.9 18.8 1.0
CAN A:EXX408 2.9 15.4 1.0
O A:HOH822 3.2 11.3 1.0
BRD A:EXX408 3.2 24.5 1.0
HB2 A:PHE113 3.4 13.8 1.0
BRE A:EXX408 3.4 22.9 1.0
HG12 A:ILE95 3.5 13.4 1.0
HG11 A:VAL66 3.5 17.2 1.0
HB A:ILE174 3.6 11.3 1.0
CG A:PHE113 3.7 11.1 1.0
HG21 A:ILE174 3.7 13.0 1.0
HD2 A:LYS68 3.7 19.1 1.0
HB3 A:PHE113 3.7 13.8 1.0
CD2 A:PHE113 3.7 11.7 1.0
HD2 A:PHE113 3.7 14.0 1.0
CB A:PHE113 3.8 11.5 1.0
HB A:VAL66 3.8 16.3 1.0
HD12 A:ILE174 3.8 14.7 1.0
HD13 A:ILE174 3.9 14.7 1.0
HG12 A:VAL66 4.1 17.2 1.0
HG22 A:ILE174 4.1 13.0 1.0
CG1 A:VAL66 4.1 14.3 1.0
CAO A:EXX408 4.2 18.1 1.0
CG2 A:ILE174 4.2 10.9 1.0
CAP A:EXX408 4.3 18.6 1.0
CD1 A:PHE113 4.3 10.8 1.0
CB A:ILE174 4.3 9.4 1.0
CD1 A:ILE174 4.3 12.3 1.0
CE2 A:PHE113 4.4 13.2 1.0
CG1 A:ILE95 4.4 11.2 1.0
HD11 A:ILE95 4.4 15.2 1.0
CB A:VAL66 4.5 13.6 1.0
HG21 A:VAL66 4.6 19.9 1.0
HG3 A:LYS68 4.6 18.7 1.0
CD A:LYS68 4.6 15.9 1.0
HD13 A:ILE95 4.6 15.2 1.0
HG21 A:ILE95 4.7 11.6 1.0
HD1 A:PHE113 4.7 13.0 1.0
CD1 A:ILE95 4.7 12.7 1.0
HE2 A:PHE113 4.8 15.8 1.0
HG13 A:ILE95 4.8 13.4 1.0
OD1 A:ASP175 4.8 17.3 1.0
CAQ A:EXX408 4.8 19.9 1.0
H A:ASP175 4.8 11.4 1.0
CE1 A:PHE113 4.9 12.6 1.0
CZ A:PHE113 4.9 11.9 1.0
HG3 A:MET163 5.0 24.9 0.5
CG1 A:ILE174 5.0 10.5 1.0

Bromine binding site 3 out of 4 in 4kwp

Go back to Bromine Binding Sites List in 4kwp
Bromine binding site 3 out of 4 in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br408

b:24.5
occ:1.00
 BRD A:EXX408 0.0 24.5 1.0
CAM A:EXX408 1.9 18.8 1.0
CAL A:EXX408 2.8 18.6 1.0
CAO A:EXX408 2.9 18.1 1.0
O A:GLU114 3.0 17.6 1.0
HD11 A:ILE95 3.1 15.2 1.0
HG21 A:VAL66 3.1 19.9 1.0
BRC A:EXX408 3.2 28.4 1.0
BRF A:EXX408 3.3 26.1 1.0
HG23 A:VAL116 3.3 20.6 1.0
H A:VAL116 3.4 19.7 1.0
HA A:HIS115 3.4 17.0 1.0
HB A:VAL66 3.5 16.3 1.0
HD13 A:ILE95 3.7 15.2 1.0
CG2 A:VAL66 3.8 16.6 1.0
HG23 A:VAL66 3.8 19.9 1.0
CD1 A:ILE95 3.8 12.7 1.0
N A:VAL116 3.9 16.4 1.0
HB A:VAL116 4.0 19.0 1.0
HG21 A:ILE174 4.0 13.0 1.0
HG3 A:MET163 4.0 16.8 0.5
HG3 A:MET163 4.0 24.9 0.5
HB2 A:PHE113 4.0 13.8 1.0
HG12 A:ILE95 4.1 13.4 1.0
HG11 A:VAL66 4.1 17.2 1.0
CB A:VAL66 4.1 13.6 1.0
CAN A:EXX408 4.1 15.4 1.0
HB3 A:PHE113 4.1 13.8 1.0
CG2 A:VAL116 4.2 17.1 1.0
C A:GLU114 4.2 13.8 1.0
CA A:HIS115 4.2 14.2 1.0
CAQ A:EXX408 4.3 19.9 1.0
HG21 A:VAL116 4.3 20.6 1.0
HE2 A:MET163 4.4 13.2 0.5
C A:HIS115 4.4 14.6 1.0
CB A:VAL116 4.5 15.9 1.0
CG1 A:ILE95 4.5 11.2 1.0
HD12 A:ILE95 4.6 15.2 1.0
CB A:PHE113 4.6 11.5 1.0
HG22 A:ILE174 4.6 13.0 1.0
CG1 A:VAL66 4.6 14.3 1.0
HG22 A:VAL66 4.6 19.9 1.0
N A:HIS115 4.7 13.7 1.0
CAP A:EXX408 4.7 18.6 1.0
CG2 A:ILE174 4.7 10.9 1.0
CA A:VAL116 4.8 18.7 1.0
HD13 A:ILE174 4.9 14.7 1.0
HG3 A:GLU114 4.9 23.4 1.0
HG13 A:ILE95 4.9 13.4 1.0
HG22 A:VAL116 4.9 20.6 1.0
CG A:MET163 5.0 14.0 0.5
CG A:MET163 5.0 20.8 0.5

Bromine binding site 4 out of 4 in 4kwp

Go back to Bromine Binding Sites List in 4kwp
Bromine binding site 4 out of 4 in the Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Crystal Structure of Human CK2-Alpha in Complex with A Benzimidazole Inhibitor (K164) at 1.25 A Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br408

b:26.1
occ:1.00
 BRF A:EXX408 0.0 26.1 1.0
CAO A:EXX408 1.9 18.1 1.0
HE2 A:MET163 2.4 13.2 0.5
CAM A:EXX408 2.9 18.8 1.0
H A:VAL116 2.9 19.7 1.0
CAQ A:EXX408 2.9 19.9 1.0
O A:VAL116 3.0 19.0 1.0
HG21 A:VAL66 3.2 19.9 1.0
HB A:VAL116 3.3 19.0 1.0
CE A:MET163 3.3 11.0 0.5
BRD A:EXX408 3.3 24.5 1.0
CAT A:EXX408 3.4 36.1 1.0
NAU A:EXX408 3.5 22.9 1.0
HE3 A:MET163 3.5 13.2 0.5
HE1 A:MET163 3.5 13.2 0.5
N A:VAL116 3.7 16.4 1.0
HG3 A:MET163 3.8 16.8 0.5
C A:VAL116 3.9 18.3 1.0
HB2 A:ASN118 3.9 21.9 1.0
HD2 A:HIS115 4.0 29.9 1.0
CG2 A:VAL66 4.1 16.6 1.0
CB A:VAL116 4.1 15.9 1.0
HG3 A:MET163 4.1 24.9 0.5
CA A:VAL116 4.1 18.7 1.0
CAL A:EXX408 4.1 18.6 1.0
CAP A:EXX408 4.2 18.6 1.0
HB3 A:ASN118 4.2 21.9 1.0
CD2 A:HIS115 4.2 25.0 1.0
H A:ASN118 4.2 24.1 1.0
HG23 A:VAL66 4.2 19.9 1.0
HA A:HIS115 4.3 17.0 1.0
OAK A:EXX408 4.3 46.2 1.0
HB3 A:MET163 4.3 17.9 0.5
HG22 A:VAL66 4.4 19.9 1.0
HB3 A:MET163 4.4 15.5 0.5
HE2 A:HIS115 4.4 27.9 1.0
SD A:MET163 4.4 12.3 0.5
NE2 A:HIS115 4.4 23.3 1.0
CG A:MET163 4.5 14.0 0.5
CAI A:EXX408 4.5 39.0 1.0
HE3 A:MET163 4.5 15.0 0.5
HG23 A:VAL116 4.5 20.6 1.0
CB A:ASN118 4.5 18.2 1.0
CAN A:EXX408 4.6 15.4 1.0
SD A:MET163 4.7 23.9 0.5
CG A:MET163 4.7 20.8 0.5
CAG A:EXX408 4.8 24.3 1.0
C A:HIS115 4.8 14.6 1.0
CG2 A:VAL116 4.8 17.1 1.0
CG A:HIS115 4.9 19.9 1.0
O A:HOH866 4.9 39.2 1.0
HG11 A:VAL66 4.9 17.2 1.0
N A:ASN118 5.0 20.1 1.0
CB A:MET163 5.0 12.9 0.5
CA A:HIS115 5.0 14.2 1.0

Reference:

G.Cozza, C.Girardi, A.Ranchio, G.Lolli, S.Sarno, A.Orzeszko, Z.Kazimierczuk, R.Battistutta, M.Ruzzene, L.A.Pinna. Cell-Permeable Dual Inhibitors of Protein Kinases CK2 and Pim-1: Structural Features and Pharmacological Potential. Cell.Mol.Life Sci. V. 71 3173 2014.
ISSN: ISSN 1420-682X
PubMed: 24442476
DOI: 10.1007/S00018-013-1552-5
Page generated: Wed Jul 10 21:54:36 2024

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