Zinc in PDB 4krs: Tankyrase-1 Complexed with Small Molecule Inhibitor

All present enzymatic activity of Tankyrase-1 Complexed with Small Molecule Inhibitor:
2.4.2.30;

The structure of Tankyrase-1 Complexed with Small Molecule Inhibitor, PDB code: 4krs was solved by T.Stams, C.Kirby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.90 / 2.29
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	124.594, 44.233, 87.845, 90.00, 90.14, 90.00
R / Rfree (%)	20.7 / 26.9

The binding sites of Zinc atom in the Tankyrase-1 Complexed with Small Molecule Inhibitor (pdb code 4krs). 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-1 Complexed with Small Molecule Inhibitor, PDB code: 4krs:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Tankyrase-1 Complexed with Small Molecule Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Tankyrase-1 Complexed with Small Molecule Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1401 b:38.2 occ:1.00 ND1 A:HIS1237 2.2 46.6 1.0 SG A:CYS1245 2.3 36.0 1.0 SG A:CYS1242 2.3 37.9 1.0 SG A:CYS1234 2.4 33.0 1.0 CE1 A:HIS1237 3.2 38.4 1.0 CB A:CYS1234 3.3 41.0 1.0 CG A:HIS1237 3.3 41.0 1.0 CB A:CYS1245 3.3 33.4 1.0 CB A:CYS1242 3.4 33.1 1.0 CB A:HIS1237 3.6 33.2 1.0 N A:HIS1237 4.0 40.7 1.0 N A:CYS1245 4.1 36.1 1.0 NE2 A:HIS1237 4.3 44.9 1.0 CA A:CYS1245 4.3 36.7 1.0 O A:HOH1529 4.3 44.0 1.0 CD2 A:HIS1237 4.4 44.7 1.0 CA A:HIS1237 4.4 39.9 1.0 CB A:THR1236 4.5 43.6 1.0 CA A:CYS1234 4.7 36.8 1.0 CA A:CYS1242 4.8 33.1 1.0 C A:THR1236 5.0 45.2 1.0

Zinc binding site 2 out of 2 in the Tankyrase-1 Complexed with Small Molecule Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Tankyrase-1 Complexed with Small Molecule Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1401 b:40.7 occ:1.00 SG B:CYS1242 2.3 41.7 1.0 SG B:CYS1245 2.3 47.1 1.0 ND1 B:HIS1237 2.3 41.1 1.0 SG B:CYS1234 2.5 39.6 1.0 CG B:HIS1237 3.2 41.7 1.0 CE1 B:HIS1237 3.2 37.0 1.0 CB B:CYS1245 3.3 38.3 1.0 CB B:CYS1234 3.3 39.2 1.0 CB B:CYS1242 3.4 40.6 1.0 CB B:HIS1237 3.5 40.9 1.0 N B:CYS1245 3.9 37.4 1.0 N B:HIS1237 4.0 39.1 1.0 CA B:CYS1245 4.2 37.5 1.0 NE2 B:HIS1237 4.3 45.0 1.0 CD2 B:HIS1237 4.3 44.4 1.0 CA B:HIS1237 4.4 37.7 1.0 O B:HOH1539 4.6 40.3 1.0 CB B:THR1236 4.6 42.6 1.0 O B:HOH1534 4.6 42.8 1.0 CB B:ILE1244 4.6 38.5 1.0 CA B:CYS1234 4.8 41.9 1.0 CA B:CYS1242 4.8 38.9 1.0 C B:THR1236 4.9 44.5 1.0 C B:ILE1244 5.0 37.0 1.0 N B:THR1236 5.0 43.4 1.0

M.D.Shultz, D.Majumdar, D.N.Chin, P.D.Fortin, Y.Feng, T.Gould, C.A.Kirby, T.Stams, N.J.Waters, W.Shao. Structure-Efficiency Relationship of [1,2,4]Triazol-3-Ylamines As Novel Nicotinamide Isosteres That Inhibit Tankyrases. J.Med.Chem. V. 56 7049 2013.
ISSN: ISSN 0022-2623
PubMed: 23879431
DOI: 10.1021/JM400826J