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Magnesium in PDB 2wvj: Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
Enzymatic activity of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
All present enzymatic activity of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine:
2.7.1.21;
2.7.1.21;
Protein crystallography data
The structure of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine, PDB code: 2wvj
was solved by
T.Skovgaard,
U.Uhlin,
B.Munch-Petersen,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 49.81 / 2.20 |
| Space group | C 1 2 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 156.902, 123.252, 121.024, 90.00, 132.98, 90.00 |
| R / Rfree (%) | 17.3 / 22.1 |
Other elements in 2wvj:
The structure of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine also contains other interesting chemical elements:
| Zinc | (Zn) | 8 atoms |
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
(pdb code 2wvj). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine, PDB code: 2wvj:
Jump to Magnesium binding site number: 1; 2; 3;
In total 3 binding sites of Magnesium where determined in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine, PDB code: 2wvj:
Jump to Magnesium binding site number: 1; 2; 3;
Magnesium binding site 1 out of 3 in 2wvj
Go back to
Magnesium Binding Sites List in 2wvj
Magnesium binding site 1 out
of 3 in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine within 5.0Å range:
|
Magnesium binding site 2 out of 3 in 2wvj
Go back to
Magnesium Binding Sites List in 2wvj
Magnesium binding site 2 out
of 3 in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine within 5.0Å range:
|
Magnesium binding site 3 out of 3 in 2wvj
Go back to
Magnesium Binding Sites List in 2wvj
Magnesium binding site 3 out
of 3 in the Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of Mutation of THR163 to Ser in Human Thymidine Kinase Shifts the Specificity From Thymidine Towards the Nucleoside Analogue Azidothymidine within 5.0Å range:
|
Reference:
T.Skovgaard,
U.Uhlin,
B.Munch-Petersen.
Comparative Active-Site Mutation Study of Human and Caenorhabditis Elegans Thymidine Kinase 1. Febs J. V. 279 1777 2012.
ISSN: ISSN 1742-464X
PubMed: 22385435
DOI: 10.1111/J.1742-4658.2012.08554.X
Page generated: Wed Aug 14 06:17:38 2024
ISSN: ISSN 1742-464X
PubMed: 22385435
DOI: 10.1111/J.1742-4658.2012.08554.X
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