Zinc in PDB 7r3z: Tankyrase 2 Catalytic Domain in Complex with OUL40

All present enzymatic activity of Tankyrase 2 Catalytic Domain in Complex with OUL40:
2.4.2.30;

The structure of Tankyrase 2 Catalytic Domain in Complex with OUL40, PDB code: 7r3z was solved by S.Murthy, H.Venkannagari, M.M.Maksimainen, L.Lehtio, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.02 / 2.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	91.96, 97.49, 117.9, 90, 90, 90
R / Rfree (%)	19.7 / 24.5

The binding sites of Zinc atom in the Tankyrase 2 Catalytic Domain in Complex with OUL40 (pdb code 7r3z). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Tankyrase 2 Catalytic Domain in Complex with OUL40, PDB code: 7r3z:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Tankyrase 2 Catalytic Domain in Complex with OUL40


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tankyrase 2 Catalytic Domain in Complex with OUL40 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1204 b:45.7 occ:1.00 SG A:CYS1081 2.2 43.1 1.0 SG A:CYS1092 2.2 51.1 1.0 SG A:CYS1089 2.3 42.4 1.0 ND1 A:HIS1084 2.4 48.1 1.0 CB A:CYS1081 3.0 47.7 1.0 CB A:CYS1089 3.1 36.9 1.0 CB A:CYS1092 3.2 45.7 1.0 CE1 A:HIS1084 3.3 54.3 1.0 CG A:HIS1084 3.3 48.5 1.0 CB A:HIS1084 3.6 47.9 1.0 N A:HIS1084 3.9 46.0 1.0 N A:CYS1092 4.0 40.5 1.0 CA A:CYS1092 4.2 43.6 1.0 CA A:HIS1084 4.4 45.9 1.0 NE2 A:HIS1084 4.4 54.8 1.0 CD2 A:HIS1084 4.4 54.5 1.0 CA A:CYS1081 4.5 48.8 1.0 CA A:CYS1089 4.6 37.7 1.0 CB A:VAL1083 4.7 51.3 1.0 O A:HOH1309 4.7 44.9 1.0 CB A:ILE1091 4.8 43.5 1.0 C A:VAL1083 4.8 47.4 1.0 N A:VAL1083 4.9 49.7 1.0 C A:CYS1081 4.9 50.1 1.0

Zinc binding site 2 out of 2 in the Tankyrase 2 Catalytic Domain in Complex with OUL40


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Tankyrase 2 Catalytic Domain in Complex with OUL40 within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1204 b:43.3 occ:1.00 SG B:CYS1092 2.1 51.7 1.0 ND1 B:HIS1084 2.2 50.6 1.0 SG B:CYS1089 2.3 37.3 1.0 SG B:CYS1081 2.4 40.6 1.0 CE1 B:HIS1084 3.0 54.0 1.0 CB B:CYS1081 3.0 41.9 1.0 CB B:CYS1092 3.1 44.5 1.0 CB B:CYS1089 3.2 35.6 1.0 CG B:HIS1084 3.3 48.4 1.0 CB B:HIS1084 3.6 45.0 1.0 N B:HIS1084 3.9 45.6 1.0 N B:CYS1092 4.0 40.3 1.0 CA B:CYS1092 4.1 44.8 1.0 O B:HOH1334 4.2 45.9 1.0 NE2 B:HIS1084 4.2 52.9 1.0 CD2 B:HIS1084 4.3 51.5 1.0 CB B:VAL1083 4.3 50.1 1.0 CA B:HIS1084 4.4 45.5 1.0 CA B:CYS1081 4.5 42.1 1.0 CA B:CYS1089 4.7 34.7 1.0 C B:VAL1083 4.8 43.7 1.0 CG1 B:VAL1083 4.8 51.0 1.0 N B:VAL1083 4.8 46.8 1.0 O B:HOH1302 4.8 43.3 1.0 CB B:ILE1091 4.9 43.9 1.0 CA B:VAL1083 4.9 47.6 1.0 C B:CYS1081 5.0 42.8 1.0

S.Murthy, M.G.Nizi, M.M.Maksimainen, S.Massari, J.Alaviuhkola, B.E.Lippok, C.Vagaggini, S.T.Sowa, A.Galera-Prat, Y.Ashok, H.Venkannagari, R.Prunskaite-Hyyrylainen, E.Dreassi, B.Luscher, P.Korn, O.Tabarrini, L.Lehtio. [1,2,4]Triazolo[3,4- B ]Benzothiazole Scaffold As Versatile Nicotinamide Mimic Allowing Nanomolar Inhibition of Different Parp Enzymes. J.Med.Chem. 2023.
ISSN: ISSN 0022-2623
PubMed: 36598465
DOI: 10.1021/ACS.JMEDCHEM.2C01460