Zinc in PDB 5lbz: Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib

All present enzymatic activity of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib:
1.10.5.1;

The structure of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib, PDB code: 5lbz was solved by S.Schneider, G.Medard, B.Kuster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.60 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.454, 79.220, 106.230, 90.00, 90.00, 90.00
R / Rfree (%)	10.9 / 13.1

The binding sites of Zinc atom in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib (pdb code 5lbz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib, PDB code: 5lbz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn305 b:11.0 occ:0.50 O A:CYS222 2.1 24.0 0.3 O A:CYS222 2.1 16.5 0.7 SG A:CYS222 2.2 11.5 0.7 ND1 A:HIS173 2.3 14.4 1.0 ND1 A:HIS177 2.3 16.2 1.0 CB A:CYS222 2.6 14.4 0.3 CB A:CYS222 2.7 15.4 0.7 C A:CYS222 2.9 14.3 0.3 C A:CYS222 2.9 14.6 0.7 CG A:HIS177 3.1 8.5 1.0 CG A:HIS173 3.2 9.8 1.0 CE1 A:HIS173 3.3 15.6 1.0 CB A:HIS177 3.3 7.6 1.0 CA A:CYS222 3.3 15.6 0.3 CA A:CYS222 3.4 13.7 0.7 CE1 A:HIS177 3.4 19.0 1.0 CB A:HIS173 3.4 8.7 1.0 CA A:HIS173 3.5 7.0 1.0 SG A:CYS222 3.7 10.1 0.3 N A:THR223 4.1 9.6 1.0 CD2 A:HIS177 4.3 11.1 1.0 CD2 A:HIS173 4.4 10.5 1.0 N A:HIS173 4.4 7.3 1.0 NE2 A:HIS177 4.4 14.8 1.0 NE2 A:HIS173 4.4 11.3 1.0 O A:GLN172 4.4 9.5 1.0 O A:HOH595 4.5 30.3 1.0 O A:HOH589 4.5 26.6 1.0 N A:CYS222 4.5 15.3 0.3 N A:CYS222 4.5 17.0 0.7 C A:HIS173 4.5 7.7 1.0 O A:HIS173 4.6 8.1 1.0 CA A:THR223 4.7 10.4 1.0 C A:GLN172 4.7 7.3 1.0 CA A:HIS177 4.8 6.8 1.0 O A:HOH543 4.9 20.1 1.0

Zinc binding site 2 out of 2 in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Pacritinib within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn305 b:23.4 occ:0.50 O B:CYS222 2.0 23.4 0.6 ND1 B:HIS177 2.3 23.0 1.0 SG B:CYS222 2.4 15.4 0.6 ND1 B:HIS173 2.4 19.4 1.0 O B:CYS222 2.5 24.2 0.4 CB B:CYS222 2.7 20.9 0.4 CB B:CYS222 3.0 17.2 0.6 C B:CYS222 3.1 22.7 0.6 CG B:HIS177 3.1 13.1 1.0 C B:CYS222 3.1 20.1 0.4 CG B:HIS173 3.3 10.2 1.0 CE1 B:HIS177 3.3 23.9 1.0 CB B:HIS177 3.3 9.9 1.0 CE1 B:HIS173 3.4 19.6 1.0 CA B:CYS222 3.5 17.6 0.4 CB B:HIS173 3.5 9.3 1.0 CA B:HIS173 3.6 9.4 1.0 CA B:CYS222 3.6 18.0 0.6 SG B:CYS222 3.6 22.1 0.4 N B:THR223 4.2 14.5 1.0 CD2 B:HIS177 4.2 18.6 1.0 NE2 B:HIS177 4.3 23.6 1.0 CD2 B:HIS173 4.4 11.3 1.0 NE2 B:HIS173 4.4 11.8 1.0 N B:HIS173 4.5 9.7 1.0 O B:GLN172 4.5 10.8 1.0 C B:HIS173 4.6 7.6 1.0 O B:HIS173 4.6 8.8 1.0 N B:CYS222 4.7 18.5 0.6 N B:CYS222 4.7 18.6 0.4 CA B:THR223 4.8 16.3 1.0 C B:GLN172 4.9 8.9 1.0 CA B:HIS177 4.9 7.9 1.0

S.Klaeger, S.Heinzlmeir, M.Wilhelm, H.Polzer, B.Vick, P.A.Koenig, M.Reinecke, B.Ruprecht, S.Petzoldt, C.Meng, J.Zecha, K.Reiter, H.Qiao, D.Helm, H.Koch, M.Schoof, G.Canevari, E.Casale, S.R.Depaolini, A.Feuchtinger, Z.Wu, T.Schmidt, L.Rueckert, W.Becker, J.Huenges, A.K.Garz, B.O.Gohlke, D.P.Zolg, G.Kayser, T.Vooder, R.Preissner, H.Hahne, N.Tonisson, K.Kramer, K.Gotze, F.Bassermann, J.Schlegl, H.C.Ehrlich, S.Aiche, A.Walch, P.A.Greif, S.Schneider, E.R.Felder, J.Ruland, G.Medard, I.Jeremias, K.Spiekermann, B.Kuster. The Target Landscape of Clinical Kinase Drugs. Science V. 358 2017.
ISSN: ESSN 1095-9203
PubMed: 29191878
DOI: 10.1126/SCIENCE.AAN4368