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

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

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

Resolution Low / High (Å)	44.30 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.586, 79.401, 106.571, 90.00, 90.00, 90.00
R / Rfree (%)	10.5 / 12.5

The binding sites of Zinc atom in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Crenolanib (pdb code 5lby). 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 Crenolanib, PDB code: 5lby:
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 Crenolanib


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 Crenolanib within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:7.6 occ:0.70 ND1 A:HIS177 2.1 11.6 1.0 O A:CYS222 2.1 11.4 1.0 ND1 A:HIS173 2.1 12.1 1.0 SG A:CYS222 2.3 12.0 1.0 CB A:CYS222 2.9 11.3 1.0 C A:CYS222 2.9 10.2 1.0 CG A:HIS177 3.0 8.8 1.0 CE1 A:HIS177 3.0 13.4 1.0 CE1 A:HIS173 3.1 12.5 1.0 CG A:HIS173 3.1 10.9 1.0 CB A:HIS177 3.3 8.6 1.0 CA A:CYS222 3.4 12.0 1.0 CB A:HIS173 3.4 10.4 1.0 CA A:HIS173 3.6 9.2 1.0 N A:THR223 4.0 10.0 1.0 NE2 A:HIS177 4.1 12.2 1.0 CD2 A:HIS177 4.2 9.9 1.0 NE2 A:HIS173 4.2 13.0 1.0 CD2 A:HIS173 4.2 12.1 1.0 N A:HIS173 4.6 9.2 1.0 N A:CYS222 4.6 11.2 1.0 C A:HIS173 4.6 9.6 1.0 CA A:THR223 4.6 10.4 1.0 O A:HIS173 4.6 9.4 1.0 O A:HOH606 4.6 24.8 1.0 O A:GLN172 4.7 10.0 1.0 O A:HOH595 4.8 24.6 1.0 CA A:HIS177 4.8 8.0 1.0 O A:HOH548 4.8 18.0 1.0 C A:GLN172 5.0 8.7 1.0

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


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 Crenolanib within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn302 b:9.2 occ:0.70 O B:CYS222 2.0 12.9 1.0 ND1 B:HIS173 2.1 12.8 1.0 ND1 B:HIS177 2.1 13.8 1.0 SG B:CYS222 2.3 12.8 1.0 CB B:CYS222 2.8 12.6 1.0 C B:CYS222 2.9 12.1 1.0 CG B:HIS177 3.0 10.9 1.0 CE1 B:HIS173 3.1 13.2 1.0 CG B:HIS173 3.1 10.7 1.0 CE1 B:HIS177 3.1 14.5 1.0 CB B:HIS177 3.2 10.6 1.0 CB B:HIS173 3.4 10.0 1.0 CA B:CYS222 3.4 13.6 1.0 CA B:HIS173 3.6 9.8 1.0 N B:THR223 4.0 13.2 1.0 NE2 B:HIS173 4.2 12.9 1.0 CD2 B:HIS177 4.2 13.8 1.0 CD2 B:HIS173 4.2 11.1 1.0 NE2 B:HIS177 4.2 15.1 1.0 N B:CYS222 4.5 12.9 1.0 N B:HIS173 4.6 10.0 1.0 C B:HIS173 4.6 9.4 1.0 CA B:THR223 4.6 13.8 1.0 O B:HIS173 4.6 10.5 1.0 O B:GLN172 4.7 10.6 1.0 CA B:HIS177 4.8 9.7 1.0 O B:HOH588 4.9 29.1 1.0 C B:GLN172 5.0 9.8 1.0 CE1 B:HIS227 5.0 11.3 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