Zinc in PDB 5fpf: Crystal Structure of Human Tankyrase 2 in Complex with Ta-91

The structure of Crystal Structure of Human Tankyrase 2 in Complex with Ta-91, PDB code: 5fpf 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)	29.42 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	41.600, 76.080, 149.050, 90.00, 90.00, 90.00
R / Rfree (%)	21.3 / 27.2

The binding sites of Zinc atom in the Crystal Structure of Human Tankyrase 2 in Complex with Ta-91 (pdb code 5fpf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Tankyrase 2 in Complex with Ta-91, PDB code: 5fpf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Tankyrase 2 in Complex with Ta-91


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 Ta-91 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn2111 b:52.0 occ:1.00 HD1 A:HIS1084 1.8 68.5 1.0 SG A:CYS1092 2.3 53.2 1.0 SG A:CYS1081 2.3 63.9 1.0 SG A:CYS1089 2.3 48.7 1.0 ND1 A:HIS1084 2.4 57.1 1.0 HB2 A:HIS1084 2.6 72.4 1.0 HB2 A:CYS1089 3.1 58.9 1.0 H A:HIS1084 3.1 71.1 1.0 CG A:HIS1084 3.2 58.0 1.0 CB A:CYS1089 3.2 49.1 1.0 HB2 A:CYS1081 3.2 68.2 1.0 HB2 A:CYS1092 3.2 57.6 1.0 CB A:CYS1081 3.3 56.8 1.0 H A:CYS1092 3.3 51.4 1.0 CB A:HIS1084 3.3 60.3 1.0 CB A:CYS1092 3.4 48.0 1.0 CE1 A:HIS1084 3.4 54.0 1.0 HB3 A:CYS1089 3.4 58.9 1.0 HB3 A:CYS1081 3.5 68.2 1.0 HB A:VAL1083 3.6 73.2 1.0 HE1 A:HIS1084 3.7 64.8 1.0 HB A:ILE1091 3.7 52.9 1.0 N A:HIS1084 3.8 59.2 1.0 N A:CYS1092 4.0 42.9 1.0 HB3 A:HIS1084 4.1 72.4 1.0 HB3 A:CYS1092 4.1 57.6 1.0 CA A:HIS1084 4.2 59.5 1.0 CD2 A:HIS1084 4.3 55.8 1.0 CA A:CYS1092 4.3 46.4 1.0 NE2 A:HIS1084 4.4 55.9 1.0 HG13 A:VAL1083 4.4 72.5 1.0 HB3 A:ASP1086 4.5 70.0 1.0 H A:VAL1083 4.5 75.6 1.0 CB A:VAL1083 4.5 61.0 1.0 HD13 A:ILE1091 4.5 54.7 1.0 H A:ASP1086 4.6 70.7 1.0 H A:ILE1091 4.6 52.5 1.0 CA A:CYS1089 4.6 48.2 1.0 CA A:CYS1081 4.7 56.7 1.0 CB A:ILE1091 4.7 44.0 1.0 HA A:CYS1089 4.7 57.9 1.0 HA A:CYS1092 4.7 55.7 1.0 C A:VAL1083 4.8 59.9 1.0 CG1 A:VAL1083 4.9 60.4 1.0 HG12 A:VAL1083 4.9 72.5 1.0 HA A:HIS1084 4.9 71.4 1.0 H A:CYS1081 4.9 68.0 1.0 N A:VAL1083 5.0 63.0 1.0 C A:HIS1084 5.0 59.2 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Tankyrase 2 in Complex with Ta-91


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Tankyrase 2 in Complex with Ta-91 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn2111 b:67.6 occ:1.00 ND1 B:HIS1084 2.2 59.4 1.0 SG B:CYS1089 2.3 52.3 1.0 SG B:CYS1092 2.5 54.0 1.0 SG B:CYS1081 2.5 61.3 1.0 CE1 B:HIS1084 3.0 56.3 1.0 HB2 B:HIS1084 3.0 68.8 1.0 HB2 B:CYS1081 3.1 70.7 1.0 HB2 B:CYS1089 3.1 67.0 1.0 HB2 B:CYS1092 3.2 58.6 1.0 CG B:HIS1084 3.2 60.1 1.0 HE1 B:HIS1084 3.2 67.6 1.0 CB B:CYS1089 3.2 55.8 1.0 H B:CYS1092 3.2 58.1 1.0 CB B:CYS1081 3.2 58.9 1.0 HB3 B:CYS1089 3.3 67.0 1.0 HB3 B:CYS1081 3.4 70.7 1.0 CB B:CYS1092 3.4 48.9 1.0 CB B:HIS1084 3.6 57.3 1.0 H B:HIS1084 3.6 71.9 1.0 HB B:VAL1083 3.6 71.1 1.0 HB B:ILE1091 3.7 59.9 1.0 N B:CYS1092 3.9 48.5 1.0 NE2 B:HIS1084 4.1 56.5 1.0 N B:HIS1084 4.1 59.9 1.0 CD2 B:HIS1084 4.2 57.8 1.0 HB3 B:CYS1092 4.2 58.6 1.0 H B:VAL1083 4.2 69.9 1.0 CA B:CYS1092 4.3 45.9 1.0 HB3 B:ASP1086 4.3 71.0 1.0 HB3 B:HIS1084 4.4 68.8 1.0 CA B:HIS1084 4.5 58.6 1.0 H B:ILE1091 4.5 58.1 1.0 CB B:VAL1083 4.6 59.3 1.0 H B:ASP1086 4.6 69.5 1.0 CA B:CYS1089 4.7 55.8 1.0 CA B:CYS1081 4.7 56.4 1.0 CB B:ILE1091 4.7 49.9 1.0 HA B:CYS1092 4.7 55.1 1.0 HD13 B:ILE1091 4.7 60.1 1.0 HE2 B:HIS1084 4.8 67.8 1.0 HA B:CYS1089 4.8 67.0 1.0 C B:VAL1083 4.9 60.0 1.0 N B:VAL1083 4.9 58.2 1.0 H B:CYS1081 5.0 67.2 1.0 HD2 B:HIS1084 5.0 69.4 1.0

A.Nathubhai, T.Haikarainen, P.C.Hayward, S.Munoz-Descalzo, D.Tosh, M.D.Lloyd, L.Lehtio, M.D.Threadgill. Design, Synthesis and Evaluation of Novel Dual- Binding Inhibitors of the Tankyrases and Wnt Signalling. To Be Published.