Zinc in PDB 5adq: Crystal Structure of Human Tankyrase 2 in Complex with JW55

The structure of Crystal Structure of Human Tankyrase 2 in Complex with JW55, PDB code: 5adq was solved by T.Haikarainen, L.Lehtio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.79 / 2.10
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.170, 66.170, 121.610, 90.00, 90.00, 90.00
R / Rfree (%)	18.797 / 23.784

The binding sites of Zinc atom in the Crystal Structure of Human Tankyrase 2 in Complex with JW55 (pdb code 5adq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Human Tankyrase 2 in Complex with JW55, PDB code: 5adq:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Tankyrase 2 in Complex with JW55


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Tankyrase 2 in Complex with JW55 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2114 b:24.1 occ:1.00 ND1 A:HIS1084 2.1 29.0 1.0 SG A:CYS1089 2.2 22.0 1.0 SG A:CYS1092 2.3 26.7 1.0 SG A:CYS1081 2.4 23.5 1.0 CE1 A:HIS1084 3.0 28.6 1.0 CB A:CYS1081 3.2 25.2 1.0 CG A:HIS1084 3.2 29.4 1.0 CB A:CYS1089 3.2 23.9 1.0 CB A:CYS1092 3.3 26.1 1.0 CB A:HIS1084 3.7 26.6 1.0 N A:HIS1084 3.9 25.8 1.0 N A:CYS1092 4.0 23.4 1.0 NE2 A:HIS1084 4.2 29.6 1.0 CA A:CYS1092 4.2 25.5 1.0 O A:HOH2081 4.3 28.4 1.0 CD2 A:HIS1084 4.3 28.7 1.0 CB A:VAL1083 4.4 26.1 1.0 CA A:HIS1084 4.4 25.9 1.0 CA A:CYS1089 4.6 24.9 1.0 CA A:CYS1081 4.7 26.6 1.0 CB A:ILE1091 4.8 24.1 1.0 N A:VAL1083 4.8 26.5 1.0 C A:VAL1083 4.8 26.1 1.0 CA A:VAL1083 4.9 26.0 1.0 O A:HOH2073 4.9 30.2 1.0 CG1 A:VAL1083 5.0 23.0 1.0

T.Haikarainen, J.Waaler, A.Ignatev, Y.Nkizinkiko, H.Venkannagari, E.Obaji, S.Krauss, L.Lehtio. Development and Structural Analysis of Adenosine Site Binding Tankyrase Inhibitors. Bioorg.Med.Chem.Lett. V. 26 328 2016.
ISSN: ISSN 0960-894X
PubMed: 26706174
DOI: 10.1016/J.BMCL.2015.12.018