Zinc in PDB 2qq0: Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine + Appnhp

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

The structure of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine + Appnhp, PDB code: 2qq0 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)	28.00 / 1.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	102.160, 59.310, 61.300, 90.00, 103.02, 90.00
R / Rfree (%)	17.1 / 21.7

The structure of Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine + Appnhp also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Zinc atom in the Thymidine Kinase From Thermotoga Maritima in Complex with Thymidine + Appnhp (pdb code 2qq0). 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 + Appnhp, PDB code: 2qq0:
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 + Appnhp


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 + Appnhp within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:20.0 occ:1.00 SG A:CYS140 2.3 16.2 1.0 SG A:CYS173 2.3 18.1 1.0 SG A:CYS143 2.4 21.3 1.0 SG A:CYS176 2.5 21.5 1.0 CB A:CYS140 3.1 16.3 1.0 CB A:CYS176 3.3 17.9 1.0 CB A:CYS143 3.3 21.4 1.0 CB A:CYS173 3.5 13.9 1.0 N A:CYS143 3.8 21.1 1.0 N A:CYS173 3.9 12.2 1.0 OD1 A:ASN147 4.1 20.4 1.0 CA A:CYS143 4.1 21.1 1.0 CA A:CYS173 4.2 13.9 1.0 N A:CYS176 4.4 17.4 1.0 CA A:CYS176 4.4 17.7 1.0 CA A:CYS140 4.6 14.7 1.0 ND2 A:ASN147 4.6 25.9 1.0 CB A:ARG142 4.7 20.3 1.0 CG A:ASN147 4.8 17.9 1.0 C A:ARG142 4.8 21.7 1.0 C A:CYS173 4.9 14.6 1.0 O A:CYS173 4.9 15.9 1.0 C A:CYS143 5.0 20.8 1.0

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


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 + Appnhp within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:19.7 occ:1.00 SG B:CYS176 2.3 21.7 1.0 SG B:CYS143 2.3 21.8 1.0 SG B:CYS140 2.4 16.0 1.0 SG B:CYS173 2.4 17.6 1.0 CB B:CYS140 3.2 14.7 1.0 CB B:CYS176 3.2 18.4 1.0 CB B:CYS143 3.3 20.4 1.0 CB B:CYS173 3.6 13.2 1.0 N B:CYS143 3.7 20.6 1.0 N B:CYS173 4.0 11.9 1.0 CA B:CYS143 4.1 20.8 1.0 OD1 B:ASN147 4.2 17.2 1.0 CA B:CYS173 4.3 13.3 1.0 O B:HOH824 4.4 35.3 1.0 CA B:CYS176 4.4 18.1 1.0 N B:CYS176 4.4 17.2 1.0 ND2 B:ASN147 4.5 25.3 1.0 O B:HOH813 4.6 42.7 1.0 CB B:ARG142 4.6 21.1 1.0 CA B:CYS140 4.7 14.1 1.0 C B:ARG142 4.8 21.8 1.0 CG B:ASN147 4.8 16.8 1.0 C B:CYS143 4.9 20.5 1.0 C B:CYS173 5.0 13.1 1.0 O B:CYS173 5.0 14.0 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