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

Enzymatic activity of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Volitinib

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

Protein crystallography data

The structure of Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Volitinib, PDB code: 5lbw 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) 44.50 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.398, 81.372, 106.403, 90.00, 90.00, 90.00
R / Rfree (%) 25.3 / 27.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Volitinib (pdb code 5lbw). 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 Volitinib, PDB code: 5lbw:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 5lbw

Go back to Zinc Binding Sites List in 5lbw
Zinc binding site 1 out of 2 in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Volitinib


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 Volitinib within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:39.6
occ:1.00
O A:CYS222 2.2 42.9 1.0
SG A:CYS222 2.2 41.7 1.0
ND1 A:HIS173 2.2 37.8 1.0
ND1 A:HIS177 2.4 38.5 1.0
CB A:CYS222 2.8 42.1 1.0
C A:CYS222 3.0 42.2 1.0
CG A:HIS177 3.1 37.3 1.0
CE1 A:HIS173 3.2 39.0 1.0
CG A:HIS173 3.2 36.9 1.0
CB A:HIS177 3.3 35.8 1.0
CE1 A:HIS177 3.3 39.8 1.0
CA A:CYS222 3.4 42.2 1.0
CB A:HIS173 3.5 35.7 1.0
CA A:HIS173 3.7 34.7 1.0
N A:THR223 4.0 41.9 1.0
CD2 A:HIS177 4.1 38.1 1.0
NE2 A:HIS177 4.2 39.6 1.0
NE2 A:HIS173 4.3 39.1 1.0
CD2 A:HIS173 4.4 37.7 1.0
N A:HIS173 4.6 33.8 1.0
N A:CYS222 4.6 43.0 1.0
CA A:THR223 4.6 42.5 1.0
O A:GLN172 4.7 33.4 1.0
C A:HIS173 4.7 35.0 1.0
O A:HIS173 4.8 35.6 1.0
CA A:HIS177 4.8 35.2 1.0
C A:GLN172 4.9 33.3 1.0

Zinc binding site 2 out of 2 in 5lbw

Go back to Zinc Binding Sites List in 5lbw
Zinc binding site 2 out of 2 in the Structure of the Human Quinone Reductase 2 (NQO2) in Complex with Volitinib


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 Volitinib within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn302

b:41.1
occ:1.00
SG B:CYS222 2.2 41.8 1.0
O B:CYS222 2.2 45.4 1.0
ND1 B:HIS173 2.3 36.9 1.0
ND1 B:HIS177 2.4 37.3 1.0
CB B:CYS222 2.8 42.9 1.0
C B:CYS222 3.0 43.6 1.0
CG B:HIS177 3.0 36.4 1.0
CB B:HIS177 3.2 34.9 1.0
CE1 B:HIS173 3.2 37.6 1.0
CG B:HIS173 3.2 36.3 1.0
CE1 B:HIS177 3.3 38.3 1.0
CA B:CYS222 3.4 42.9 1.0
CB B:HIS173 3.5 35.8 1.0
CA B:HIS173 3.6 35.2 1.0
CD2 B:HIS177 4.0 37.4 1.0
N B:THR223 4.1 42.6 1.0
NE2 B:HIS177 4.2 38.4 1.0
NE2 B:HIS173 4.3 37.4 1.0
CD2 B:HIS173 4.4 36.6 1.0
N B:HIS173 4.5 35.0 1.0
O B:GLN172 4.6 34.8 1.0
N B:CYS222 4.6 44.0 1.0
CA B:THR223 4.6 42.8 1.0
C B:HIS173 4.6 34.7 1.0
O B:HIS173 4.7 34.6 1.0
CA B:HIS177 4.7 34.4 1.0
C B:GLN172 4.9 34.9 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: Thu Aug 21 04:35:14 2025

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