Magnesium in PDB 5uiv: Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element.

The structure of Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element., PDB code: 5uiv was solved by K.Sinha, G.S.Rule, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.59 / 2.45
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.965, 69.965, 116.161, 90.00, 90.00, 120.00
R / Rfree (%)	16.8 / 21.8

The binding sites of Magnesium atom in the Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element. (pdb code 5uiv). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element., PDB code: 5uiv:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:16.8 occ:0.50 O3B A:ADP302 1.9 33.2 1.0 O A:HOH454 2.2 39.6 1.0 OD1 A:ASP13 2.3 36.6 1.0 O A:HOH432 2.4 44.1 1.0 O A:HOH424 2.5 28.7 1.0 O A:HOH471 2.5 53.0 1.0 PB A:ADP302 3.3 35.6 1.0 CG A:ASP13 3.5 38.8 1.0 O1B A:ADP302 3.8 39.4 1.0 O A:HOH417 3.8 33.3 1.0 O A:HOH430 3.9 32.2 1.0 MG A:MG304 3.9 18.4 0.5 N A:ARG14 4.2 32.3 1.0 O2B A:ADP302 4.2 31.3 1.0 OD2 A:ASP13 4.3 51.1 1.0 CA A:ASP13 4.3 34.1 1.0 NZ A:LYS17 4.4 29.8 1.0 O3A A:ADP302 4.4 36.4 1.0 O1P A:TMP301 4.4 25.7 1.0 CB A:ASP13 4.4 33.7 1.0 O2P A:TMP301 4.6 27.8 1.0 O2A A:ADP302 4.6 34.1 1.0 C A:ASP13 4.8 35.0 1.0

Magnesium binding site 2 out of 2 in the Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Thymidylate Kinase From Candida Albicans Reveals Origin of Broad Substrate Specificity and A Novel Structural Element. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg304 b:18.4 occ:0.50 O A:HOH450 2.4 38.2 1.0 OD2 A:ASP13 2.4 51.1 1.0 O A:GLY155 2.6 37.7 1.0 OD1 A:ASP13 2.6 36.6 1.0 CG A:ASP13 2.8 38.8 1.0 OE2 A:GLU162 2.8 34.4 1.0 O A:HOH432 3.2 44.1 1.0 O A:HOH454 3.5 39.6 1.0 C A:GLY155 3.6 38.2 1.0 CD A:GLU162 3.7 35.4 1.0 MG A:MG303 3.9 16.8 0.5 N A:GLY157 4.0 34.5 1.0 OE1 A:GLU162 4.1 34.7 1.0 CB A:ASP13 4.2 33.7 1.0 CA A:TRP156 4.2 38.3 1.0 N A:TRP156 4.3 37.7 1.0 O A:HOH430 4.4 32.2 1.0 C A:TRP156 4.4 33.5 1.0 CA A:GLY155 4.7 39.9 1.0 CA A:GLY157 4.8 30.6 1.0 CG A:GLU162 4.8 32.1 1.0 O1P A:TMP301 4.9 25.7 1.0

K.Sinha, G.S.Rule. The Structure of Thymidylate Kinase From Candida Albicans Reveals A Unique Structural Element. Biochemistry V. 56 4360 2017.
ISSN: ISSN 1520-4995
PubMed: 28742342
DOI: 10.1021/ACS.BIOCHEM.7B00498