Zinc in PDB 2qqe: Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine

All present enzymatic activity of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine:
2.7.1.21;

The structure of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine, PDB code: 2qqe was solved by D.Segura-Pena, J.Lichter, M.Trani, M.Konrad, A.Lavie, S.Lutz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 1.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	111.590, 52.820, 59.310, 90.00, 107.90, 90.00
R / Rfree (%)	23.6 / 28.6

The binding sites of Zinc atom in the Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine (pdb code 2qqe). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine, PDB code: 2qqe:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:27.4 occ:1.00 SG A:CYS143 2.2 26.6 1.0 SG A:CYS140 2.3 24.4 1.0 SG A:CYS176 2.3 25.7 1.0 SG A:CYS173 2.5 21.6 1.0 CB A:CYS143 3.1 27.2 1.0 CB A:CYS176 3.3 23.9 1.0 CB A:CYS140 3.3 22.4 1.0 CB A:CYS173 3.7 21.1 1.0 N A:CYS143 3.7 26.4 1.0 N A:CYS173 4.0 20.9 1.0 CA A:CYS143 4.0 27.1 1.0 N A:CYS176 4.4 23.5 1.0 CA A:CYS176 4.4 24.7 1.0 CA A:CYS173 4.4 21.1 1.0 OD1 A:ASN147 4.5 31.6 1.0 CA A:CYS140 4.7 23.5 1.0 ND2 A:ASN147 4.7 32.0 1.0 CB A:ARG142 4.8 27.9 1.0 C A:CYS143 4.9 28.0 1.0 C A:ARG142 4.9 27.3 1.0 N A:GLY144 5.0 28.3 1.0

Zinc binding site 2 out of 2 in the Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:29.4 occ:1.00 SG B:CYS143 2.2 29.9 1.0 SG B:CYS176 2.3 28.9 1.0 SG B:CYS140 2.4 25.0 1.0 SG B:CYS173 2.4 22.4 1.0 CB B:CYS140 3.1 23.8 1.0 CB B:CYS143 3.2 28.7 1.0 CB B:CYS176 3.4 24.9 1.0 CB B:CYS173 3.5 23.3 1.0 N B:CYS143 3.8 29.0 1.0 N B:CYS173 4.0 22.1 1.0 CA B:CYS143 4.1 28.6 1.0 CA B:CYS173 4.3 21.9 1.0 OD1 B:ASN147 4.4 32.4 1.0 N B:CYS176 4.5 24.9 1.0 CA B:CYS176 4.6 24.9 1.0 CA B:CYS140 4.6 24.9 1.0 ND2 B:ASN147 4.7 29.8 1.0 CB B:ARG142 4.7 28.8 1.0 C B:ARG142 4.8 28.9 1.0 C B:CYS143 4.9 28.6 1.0 C B:CYS173 5.0 21.4 1.0 O B:CYS173 5.0 20.1 1.0 CG B:ASN147 5.0 27.2 1.0

D.Segura-Pena, J.Lichter, M.Trani, M.Konrad, A.Lavie, S.Lutz. Quaternary Structure Change As A Mechanism For the Regulation of Thymidine Kinase 1-Like Enzymes. Structure V. 15 1555 2007.
ISSN: ISSN 0969-2126
PubMed: 18073106
DOI: 10.1016/J.STR.2007.09.025