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Bromine in PDB 5cqu: Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry

Enzymatic activity of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry

All present enzymatic activity of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry:
2.7.11.1;

Protein crystallography data

The structure of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry, PDB code: 5cqu was solved by K.Niefind, A.Schnitzler, R.Swider, M.Maslyk, A.Ramos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.52 / 2.35
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.481, 46.894, 63.464, 90.00, 111.56, 90.00
R / Rfree (%) 19.6 / 25.1

Bromine Binding Sites:

The binding sites of Bromine atom in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry (pdb code 5cqu). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry, PDB code: 5cqu:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in 5cqu

Go back to Bromine Binding Sites List in 5cqu
Bromine binding site 1 out of 4 in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:50.6
occ:1.00
 BR1 A:JRJ401 0.0 50.6 1.0
C14 A:JRJ401 1.8 45.5 1.0
C16 A:JRJ401 2.8 43.3 1.0
C13 A:JRJ401 2.9 46.4 1.0
O A:VAL116 3.2 41.9 1.0
BR2 A:JRJ401 3.3 47.2 1.0
N12 A:JRJ401 3.4 50.5 1.0
SD A:MET163 3.7 46.5 1.0
N A:VAL116 4.0 40.3 1.0
CB A:VAL116 4.1 39.5 1.0
C18 A:JRJ401 4.1 45.0 1.0
C A:VAL116 4.1 41.6 1.0
CG2 A:VAL66 4.2 42.9 1.0
C22 A:JRJ401 4.2 47.0 1.0
CB A:ASN118 4.3 52.9 1.0
CG A:MET163 4.3 40.3 1.0
CA A:VAL116 4.3 40.4 1.0
O A:HOH587 4.4 43.4 1.0
N11 A:JRJ401 4.7 54.4 1.0
C20 A:JRJ401 4.7 45.4 1.0
CG1 A:VAL116 4.9 43.4 1.0
CB A:MET163 4.9 35.9 1.0
N A:ASN118 5.0 50.8 1.0

Bromine binding site 2 out of 4 in 5cqu

Go back to Bromine Binding Sites List in 5cqu
Bromine binding site 2 out of 4 in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:47.2
occ:1.00
 BR2 A:JRJ401 0.0 47.2 1.0
C16 A:JRJ401 2.0 43.3 1.0
C18 A:JRJ401 2.9 45.0 1.0
C14 A:JRJ401 2.9 45.5 1.0
O A:GLU114 3.1 43.8 1.0
BR3 A:JRJ401 3.3 59.7 1.0
BR1 A:JRJ401 3.3 50.6 1.0
CG2 A:VAL66 3.7 42.9 1.0
CD1 A:ILE95 3.8 36.2 1.0
CB A:VAL66 3.9 40.3 1.0
N A:VAL116 4.2 40.3 1.0
C A:GLU114 4.3 42.2 1.0
CG1 A:VAL66 4.3 41.2 1.0
C13 A:JRJ401 4.3 46.4 1.0
C20 A:JRJ401 4.3 45.4 1.0
CG2 A:VAL116 4.3 40.8 1.0
CB A:PHE113 4.5 37.8 1.0
CB A:VAL116 4.5 39.5 1.0
CA A:HIS115 4.5 48.5 1.0
C A:HIS115 4.6 49.6 1.0
CG1 A:ILE95 4.6 49.6 1.0
CG A:MET163 4.8 40.3 1.0
CG2 A:ILE174 4.8 36.1 1.0
C22 A:JRJ401 4.8 47.0 1.0
N A:HIS115 4.9 39.7 1.0
CA A:VAL116 4.9 40.4 1.0

Bromine binding site 3 out of 4 in 5cqu

Go back to Bromine Binding Sites List in 5cqu
Bromine binding site 3 out of 4 in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:59.7
occ:1.00
 BR3 A:JRJ401 0.0 59.7 1.0
C18 A:JRJ401 1.9 45.0 1.0
C16 A:JRJ401 2.9 43.3 1.0
C20 A:JRJ401 3.0 45.4 1.0
BR2 A:JRJ401 3.3 47.2 1.0
BR4 A:JRJ401 3.5 70.5 1.0
CD2 A:PHE113 3.5 38.0 1.0
O A:HOH591 3.5 32.1 1.0
CG A:PHE113 3.6 37.5 1.0
CB A:PHE113 3.8 37.8 1.0
CE2 A:PHE113 4.2 37.8 1.0
C14 A:JRJ401 4.2 45.5 1.0
CG1 A:VAL66 4.2 41.2 1.0
C22 A:JRJ401 4.2 47.0 1.0
CG2 A:ILE174 4.3 36.1 1.0
CD1 A:PHE113 4.3 36.7 1.0
CB A:ILE174 4.4 40.5 1.0
CG1 A:ILE95 4.4 49.6 1.0
CD1 A:ILE174 4.4 42.9 1.0
CB A:VAL66 4.6 40.3 1.0
CD1 A:ILE95 4.7 36.2 1.0
C13 A:JRJ401 4.7 46.4 1.0
CZ A:PHE113 4.8 37.0 1.0
CE1 A:PHE113 4.9 37.6 1.0
OD1 A:ASP175 4.9 48.2 1.0

Bromine binding site 4 out of 4 in 5cqu

Go back to Bromine Binding Sites List in 5cqu
Bromine binding site 4 out of 4 in the Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Monoclinic Complex Structure of Protein Kinase CK2 Catalytic Subunit with A Benzotriazole-Based Inhibitor Generated By Click-Chemistry within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br401

b:70.5
occ:1.00
 BR4 A:JRJ401 0.0 70.5 1.0
C20 A:JRJ401 2.0 45.4 1.0
C22 A:JRJ401 2.9 47.0 1.0
C18 A:JRJ401 3.0 45.0 1.0
OD1 A:ASP175 3.2 48.2 1.0
N23 A:JRJ401 3.4 51.1 1.0
BR3 A:JRJ401 3.5 59.7 1.0
CG2 A:VAL53 3.7 44.9 1.0
CD1 A:ILE174 3.9 42.9 1.0
CG1 A:VAL53 4.0 40.9 1.0
C04 A:JRJ401 4.1 55.8 1.0
CD A:LYS68 4.1 53.0 1.0
CG A:ASP175 4.2 47.4 1.0
C13 A:JRJ401 4.3 46.4 1.0
C16 A:JRJ401 4.3 43.3 1.0
O A:HOH591 4.3 32.1 1.0
OD2 A:ASP175 4.5 48.6 1.0
CB A:VAL53 4.5 47.0 1.0
CE A:LYS68 4.5 52.0 1.0
C07 A:JRJ401 4.6 95.0 1.0
N11 A:JRJ401 4.7 54.4 1.0
C03 A:JRJ401 4.7 54.2 1.0
C14 A:JRJ401 4.8 45.5 1.0
CG A:LYS68 5.0 41.5 1.0
CG1 A:ILE174 5.0 40.3 1.0

Reference:

R.Swider, M.Maslyk, J.M.Zapico, C.Coderch, R.Panchuk, N.Skorokhyd, A.Schnitzler, K.Niefind, B.De Pascual-Teresa, A.Ramos. Synthesis, Biological Activity and Structural Study of New Benzotriazole-Based Protein Kinase CK2 Inhibitors Rsc Adv V. 5 72482 2015.
ISSN: ESSN 2046-2069
DOI: 10.1039/C5RA12114K
Page generated: Wed Jul 10 23:22:43 2024

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