Bromine in PDB 4d2w: Structure of Melk in Complex with Inhibitors

All present enzymatic activity of Structure of Melk in Complex with Inhibitors:
2.7.10.2; 2.7.11.1;

The structure of Structure of Melk in Complex with Inhibitors, PDB code: 4d2w was solved by C.N.Johnson, V.Berdini, L.Beke, P.Bonnet, D.Brehmer, J.E.Coyle, P.J.Day, M.Frederickson, E.J.E.Freyne, R.A.H.J.Gilissen, C.C.F.Hamlett, S.Howard, L.Meerpoel, R.Mcmenamin, S.Patel, D.C.Rees, A.Sharff, F.Sommen, T.Wu, J.T.M.Linders, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.01 / 1.92
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	65.956, 74.947, 78.216, 85.74, 70.07, 89.94
R / Rfree (%)	20.08 / 24.68

The binding sites of Bromine atom in the Structure of Melk in Complex with Inhibitors (pdb code 4d2w). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total 4 binding sites of Bromine where determined in the Structure of Melk in Complex with Inhibitors, PDB code: 4d2w:
Jump to Bromine binding site number: 1; 2; 3; 4;

Bromine binding site 1 out of 4 in the Structure of Melk in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Structure of Melk in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ A:Br1334 b:51.2 occ:1.00 BR1 A:NF51334 0.0 51.2 1.0 C2 A:NF51334 1.9 32.7 1.0 C3 A:NF51334 2.8 25.3 1.0 C7 A:NF51334 2.8 29.0 1.0 O A:HOH2062 3.0 30.2 1.0 CD1 A:LEU86 3.6 41.4 1.0 CG2 A:ILE149 4.0 26.7 1.0 O A:HOH2076 4.0 40.7 1.0 C4 A:NF51334 4.1 22.0 1.0 C6 A:NF51334 4.1 28.2 1.0 CB A:ILE149 4.3 27.5 1.0 CD1 A:ILE149 4.4 28.4 1.0 CD A:LYS40 4.5 61.7 1.0 C5 A:NF51334 4.6 28.1 1.0 SG A:CYS70 4.7 28.3 1.0 CG A:LEU86 4.7 27.7 1.0 CD1 A:LEU139 4.8 23.8 1.0 NZ A:LYS40 4.8 60.7 1.0 CB A:LEU86 4.8 21.1 1.0 O A:HOH2055 4.8 29.1 1.0 CG1 A:ILE149 5.0 26.6 1.0

Bromine binding site 2 out of 4 in the Structure of Melk in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 2 of Structure of Melk in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ B:Br1334 b:65.5 occ:1.00 BR1 B:NF51334 0.0 65.5 1.0 C2 B:NF51334 1.9 49.8 1.0 C3 B:NF51334 2.9 46.5 1.0 C7 B:NF51334 2.9 40.8 1.0 O B:HOH2041 3.2 52.8 1.0 O B:HOH2022 3.8 42.8 1.0 CD1 B:LEU86 3.9 40.4 1.0 CG2 B:ILE149 3.9 27.3 1.0 C4 B:NF51334 4.2 42.2 1.0 C6 B:NF51334 4.2 35.3 1.0 O B:HOH2054 4.3 34.9 1.0 CB B:ILE149 4.3 25.8 1.0 CD1 B:ILE149 4.4 20.4 1.0 CD B:LYS40 4.4 55.4 1.0 CD1 B:LEU139 4.6 22.2 0.5 C5 B:NF51334 4.7 34.8 1.0 SG B:CYS70 4.8 33.4 1.0 NZ B:LYS40 4.9 55.3 1.0 CE B:LYS40 5.0 62.0 1.0 CG B:LEU86 5.0 35.2 1.0 CG1 B:ILE149 5.0 23.6 1.0

Bromine binding site 3 out of 4 in the Structure of Melk in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 3 of Structure of Melk in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ C:Br1334 b:56.5 occ:1.00 BR1 C:NF51334 0.0 56.5 1.0 C2 C:NF51334 1.9 41.6 1.0 C3 C:NF51334 2.8 38.5 1.0 C7 C:NF51334 2.8 30.4 1.0 O C:HOH2035 2.9 41.2 1.0 CD1 C:LEU86 3.8 35.0 1.0 CG2 C:ILE149 4.0 30.0 1.0 O C:HOH2042 4.0 41.6 1.0 C4 C:NF51334 4.1 35.8 1.0 C6 C:NF51334 4.1 24.1 1.0 CB C:ILE149 4.2 31.9 1.0 CD1 C:ILE149 4.3 36.2 1.0 C5 C:NF51334 4.6 31.9 1.0 CD C:LYS40 4.7 73.8 1.0 SG C:CYS70 4.7 33.9 1.0 CG C:LEU86 4.8 33.3 1.0 CD1 C:LEU139 4.9 30.9 1.0 CG1 C:ILE149 4.9 32.2 1.0 CB C:LEU86 4.9 28.9 1.0 NZ C:LYS40 4.9 68.8 1.0

Bromine binding site 4 out of 4 in the Structure of Melk in Complex with Inhibitors


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 4 of Structure of Melk in Complex with Inhibitors within 5.0Å range: probe atom residue distance (Å) B Occ D:Br1334 b:60.8 occ:1.00 BR1 D:NF51334 0.0 60.8 1.0 C2 D:NF51334 1.9 38.7 1.0 O D:HOH2038 2.3 36.9 1.0 C7 D:NF51334 2.8 26.3 1.0 C3 D:NF51334 2.9 34.7 1.0 O D:HOH2039 3.3 35.7 1.0 CD1 D:LEU86 3.9 34.6 1.0 CG2 D:ILE149 4.0 23.5 1.0 C6 D:NF51334 4.1 26.1 1.0 C4 D:NF51334 4.2 33.7 1.0 CE D:LYS40 4.3 61.6 1.0 CD1 D:LEU139 4.3 28.7 1.0 O D:HOH2040 4.4 52.7 1.0 NZ D:LYS40 4.4 70.7 1.0 CD1 D:ILE149 4.4 25.1 1.0 CB D:ILE149 4.5 21.3 1.0 O A:HOH2022 4.5 49.0 1.0 O D:HOH2052 4.6 30.8 1.0 CD D:LYS40 4.6 49.9 1.0 C5 D:NF51334 4.7 26.8 1.0 SG D:CYS70 4.8 26.7 1.0

C.N.Johnson, V.Berdini, L.Beke, P.Bonnet, D.Brehmer, J.E.Coyle, P.J.Day, M.Frederickson, E.J.E.Freyne, R.A.H.J.Gilissen, C.C.F.Hamlett, S.Howard, L.Meerpoel, R.Mcmenamin, S.Patel, D.C.Rees, A.Sharff, F.Sommen, T.Wu, J.T.M.Linders. Fragment-Based Discovery of Type I Inhibitors of Maternal Embryonic Leucine Zipper Kinase Acs Med.Chem.Lett. 2014.
ISSN: ESSN 1948-5875
DOI: 10.1021/ML5001245