Zinc in PDB 4bjb: Crystal Structure of Human Tankyrase 2 in Complex with Pj-34

All present enzymatic activity of Crystal Structure of Human Tankyrase 2 in Complex with Pj-34:
2.4.2.30;

The structure of Crystal Structure of Human Tankyrase 2 in Complex with Pj-34, PDB code: 4bjb was solved by T.Haikarainen, M.Narwal, L.Lehtio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.66 / 2.30
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.330, 66.330, 121.390, 90.00, 90.00, 90.00
R / Rfree (%)	19.927 / 25.52

The binding sites of Zinc atom in the Crystal Structure of Human Tankyrase 2 in Complex with Pj-34 (pdb code 4bjb). 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 Pj-34, PDB code: 4bjb:

Zinc binding site 1 out of 1 in the Crystal Structure of Human Tankyrase 2 in Complex with Pj-34


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 Pj-34 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2165 b:41.0 occ:1.00 SG A:CYS1089 2.1 36.9 1.0 SG A:CYS1092 2.3 46.4 1.0 ND1 A:HIS1084 2.5 59.6 1.0 SG A:CYS1081 2.6 40.3 1.0 CB A:CYS1089 3.1 37.0 1.0 CB A:CYS1092 3.2 41.3 1.0 CE1 A:HIS1084 3.4 61.3 1.0 CG A:HIS1084 3.4 56.8 1.0 CB A:CYS1081 3.4 42.6 1.0 CB A:HIS1084 3.7 46.5 1.0 N A:CYS1092 3.7 40.0 1.0 CA A:CYS1092 4.0 39.4 1.0 N A:HIS1084 4.1 39.4 1.0 O A:HOH2088 4.3 45.2 1.0 NE2 A:HIS1084 4.5 60.8 1.0 CA A:CYS1089 4.5 36.1 1.0 CB A:VAL1083 4.5 44.6 1.0 CA A:HIS1084 4.5 40.5 1.0 CD2 A:HIS1084 4.5 58.9 1.0 CB A:ILE1091 4.7 42.7 1.0 C A:ILE1091 4.8 39.1 1.0 CG1 A:VAL1083 4.9 44.1 1.0 CA A:CYS1081 4.9 45.4 1.0

T.Haikarainen, M.Narwal, P.Joensuu, L.Lehtio. Evaluation and Structural Basis For the Inhibition of Tankyrases By Parp Inhibitors. Acs Med.Chem.Lett. V. 5 18 2014.
ISSN: ISSN 1948-5875
PubMed: 24900770
DOI: 10.1021/ML400292S