Zinc in PDB 4uxh: Leishmania Major Thymidine Kinase in Complex with AP5DT

All present enzymatic activity of Leishmania Major Thymidine Kinase in Complex with AP5DT:
2.7.1.21;

The structure of Leishmania Major Thymidine Kinase in Complex with AP5DT, PDB code: 4uxh was solved by J.Timm, C.Bosch-Navarrete, E.Recio, J.E.Nettleship, H.Rada, D.Gonzalez-Pacanowska, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	55.55 / 2.40
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	64.149, 64.149, 324.600, 90.00, 90.00, 120.00
R / Rfree (%)	19.546 / 25.694

The binding sites of Zinc atom in the Leishmania Major Thymidine Kinase in Complex with AP5DT (pdb code 4uxh). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Leishmania Major Thymidine Kinase in Complex with AP5DT, PDB code: 4uxh:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Leishmania Major Thymidine Kinase in Complex with AP5DT


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Leishmania Major Thymidine Kinase in Complex with AP5DT within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1181 b:51.5 occ:1.00 SG A:CYS173 2.3 49.9 1.0 SG A:CYS143 2.3 60.0 1.0 SG A:CYS176 2.3 59.4 1.0 SG A:CYS140 2.3 57.3 1.0 CB A:CYS143 3.2 64.2 1.0 CB A:CYS140 3.3 52.6 1.0 CB A:CYS176 3.3 58.7 1.0 CB A:CYS173 3.5 47.7 1.0 N A:CYS143 3.7 63.5 1.0 N A:CYS173 4.0 42.9 1.0 CA A:CYS143 4.0 64.8 1.0 CB A:GLN146 4.3 63.9 1.0 CA A:CYS173 4.3 45.0 1.0 N A:CYS176 4.4 58.0 1.0 CA A:CYS176 4.5 57.0 1.0 CB A:MET142 4.7 66.2 1.0 CA A:CYS140 4.7 49.5 1.0 C A:CYS143 4.8 66.3 1.0 C A:MET142 4.8 66.2 1.0 N A:HIS144 4.9 64.4 1.0 C A:CYS173 5.0 46.2 1.0

Zinc binding site 2 out of 2 in the Leishmania Major Thymidine Kinase in Complex with AP5DT


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Leishmania Major Thymidine Kinase in Complex with AP5DT within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1183 b:48.6 occ:1.00 SG B:CYS143 2.3 54.2 1.0 SG B:CYS140 2.3 47.8 1.0 SG B:CYS176 2.3 58.0 1.0 SG B:CYS173 2.3 48.0 1.0 CB B:CYS143 3.2 59.2 1.0 CB B:CYS140 3.2 48.6 1.0 CB B:CYS176 3.3 57.0 1.0 CB B:CYS173 3.6 44.6 1.0 N B:CYS143 3.7 60.0 1.0 N B:CYS173 4.0 41.0 1.0 CA B:CYS143 4.0 60.3 1.0 CA B:CYS173 4.4 41.5 1.0 CB B:GLN146 4.4 62.3 1.0 N B:CYS176 4.4 56.2 1.0 CA B:CYS176 4.4 57.9 1.0 CB B:MET142 4.6 65.5 1.0 CA B:CYS140 4.7 45.7 1.0 C B:CYS143 4.8 60.8 1.0 C B:MET142 4.8 64.8 1.0 N B:HIS144 4.9 65.4 1.0 C B:CYS173 5.0 42.2 1.0

J.Timm, C.Bosch-Navarrete, E.Recio, J.E.Nettleship, H.Rada, D.Gonzalez-Pacanowska, K.S.Wilson. Structural and Kinetic Characterization of Thymidine Kinase From Leishmania Major. Plos Negl Trop Dis V. 9 3781 2015.
ISSN: ISSN 1935-2727
PubMed: 25978379
DOI: 10.1371/JOURNAL.PNTD.0003781