Zinc in PDB 2ja1: Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor.

All present enzymatic activity of Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor.:
2.7.1.21;

The structure of Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor., PDB code: 2ja1 was solved by U.Kosinska, C.Carnrot, M.P.B.Sandrini, A.R.Clausen, L.Wang, J.Piskur, S.Eriksson, H.Eklund, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.63 / 2.80
Space group	I 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	95.390, 95.390, 204.862, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 23.9

The binding sites of Zinc atom in the Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor. (pdb code 2ja1). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor., PDB code: 2ja1:

Zinc binding site 1 out of 1 in the Thymidine Kinase From B. Cereus with Ttp Bound As Phosphate Donor.


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 B. Cereus with Ttp Bound As Phosphate Donor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1192 b:56.1 occ:1.00 SG A:CYS145 2.2 54.1 1.0 SG A:CYS148 2.3 51.9 1.0 SG A:CYS183 2.4 57.5 1.0 SG A:CYS186 2.5 57.1 1.0 CB A:CYS145 3.2 54.4 1.0 CB A:CYS186 3.4 55.8 1.0 CB A:CYS183 3.4 55.0 1.0 CB A:CYS148 3.5 53.9 1.0 N A:CYS183 3.9 55.3 1.0 N A:CYS148 4.0 54.3 1.0 N A:CYS186 4.2 56.2 1.0 CA A:CYS183 4.2 55.3 1.0 CA A:CYS148 4.3 54.2 1.0 CA A:CYS186 4.4 56.0 1.0 OG A:SER150 4.4 58.4 1.0 CB A:VAL147 4.6 54.2 1.0 CA A:CYS145 4.7 54.4 1.0 C A:CYS183 4.8 55.4 1.0 O A:CYS183 4.9 55.6 1.0 C A:ARG182 5.0 55.1 1.0

U.Kosinska, C.Carnrot, M.P.B.Sandrini, A.R.Clausen, L.Wang, J.Piskur, S.Eriksson, H.Eklund. Structural Studies of Thymidine Kinases From Bacillus Anthracis and Bacillus Cereus Provide Insights Into Quaternary Structure and Conformational Changes Upon Substrate Binding Febs J. V. 274 727 2007.
ISSN: ISSN 1742-464X
PubMed: 17288553
DOI: 10.1111/J.1742-4658.2006.05617.X