Zinc in PDB 2orv: Human Thymidine Kinase 1 in Complex with TP4A

All present enzymatic activity of Human Thymidine Kinase 1 in Complex with TP4A:
2.7.1.21;

The structure of Human Thymidine Kinase 1 in Complex with TP4A, PDB code: 2orv was solved by D.Segura-Pena, S.Lutz, C.Monnerjahn, M.Konrad, A.Lavie, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.50 / 2.30
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	80.980, 80.980, 156.360, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 24.9

The binding sites of Zinc atom in the Human Thymidine Kinase 1 in Complex with TP4A (pdb code 2orv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Human Thymidine Kinase 1 in Complex with TP4A, PDB code: 2orv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Human Thymidine Kinase 1 in Complex with TP4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Thymidine Kinase 1 in Complex with TP4A within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn235 b:66.5 occ:1.00 SG A:CYS156 2.0 61.8 1.0 SG A:CYS188 2.3 64.8 1.0 SG A:CYS153 2.5 55.9 1.0 SG A:CYS185 2.5 54.8 1.0 CB A:CYS156 3.1 63.0 1.0 CB A:CYS188 3.2 62.3 1.0 CB A:CYS153 3.3 55.0 1.0 N A:CYS156 3.6 63.3 1.0 CB A:CYS185 3.7 53.8 1.0 CA A:CYS156 3.9 63.3 1.0 N A:CYS188 4.1 62.9 1.0 N A:CYS185 4.1 52.9 1.0 CA A:CYS188 4.2 62.7 1.0 CA A:CYS185 4.4 53.9 1.0 C A:GLU155 4.6 62.1 1.0 C A:CYS156 4.6 64.1 1.0 N A:PHE157 4.6 64.9 1.0 CA A:CYS153 4.7 55.1 1.0 N A:ARG158 4.9 65.0 1.0 CB A:GLU155 4.9 60.8 1.0 C A:CYS185 5.0 54.4 1.0 O A:CYS185 5.0 54.3 1.0 CB A:ARG158 5.0 64.2 1.0

Zinc binding site 2 out of 2 in the Human Thymidine Kinase 1 in Complex with TP4A


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Human Thymidine Kinase 1 in Complex with TP4A within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn235 b:60.5 occ:1.00 SG B:CYS156 2.3 59.6 1.0 SG B:CYS153 2.4 56.5 1.0 SG B:CYS188 2.4 60.8 1.0 SG B:CYS185 2.5 53.6 1.0 CB B:CYS156 3.2 62.8 1.0 CB B:CYS188 3.2 61.0 1.0 CB B:CYS153 3.3 55.3 1.0 CB B:CYS185 3.5 53.3 1.0 N B:CYS156 3.8 62.9 1.0 CA B:CYS156 4.0 62.3 1.0 N B:CYS185 4.0 53.3 1.0 N B:CYS188 4.2 61.2 1.0 CA B:CYS188 4.3 61.1 1.0 CA B:CYS185 4.3 53.2 1.0 C B:CYS156 4.5 63.1 1.0 C B:GLU155 4.6 62.2 1.0 N B:PHE157 4.6 63.7 1.0 CA B:CYS153 4.7 55.8 1.0 N B:ARG158 4.7 63.4 1.0 NH1 A:ARG18 4.8 82.3 1.0 CB B:ARG158 4.9 63.1 1.0 CB B:GLU155 4.9 61.2 1.0 C B:CYS185 4.9 53.9 1.0 CG B:ARG158 5.0 66.5 1.0

D.Segura-Pena, S.Lutz, C.Monnerjahn, M.Konrad, A.Lavie. Binding of Atp to TK1-Like Enzymes Is Associated with A Conformational Change in the Quaternary Structure. J.Mol.Biol. V. 369 129 2007.
ISSN: ISSN 0022-2836
PubMed: 17407781
DOI: 10.1016/J.JMB.2007.02.104