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

Enzymatic activity of 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;

Protein crystallography data

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

Zinc Binding Sites:

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 5lby

Go back to Zinc Binding Sites List in 5lby
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 5lby

Go back to Zinc Binding Sites List in 5lby
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

Reference:

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
Page generated: Wed Dec 16 06:28:43 2020

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