Magnesium in PDB 1e9c: Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp

All present enzymatic activity of Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp:
2.7.4.9;

The structure of Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp, PDB code: 1e9c was solved by N.Ostermann, A.Lavie, S.Padiyar, R.Brundiers, T.Veit, J.Reintein, R.S.Goody, M.Konrad, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	70.00 / 1.60
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	101.300, 101.300, 49.200, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 26.8

The binding sites of Magnesium atom in the Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp (pdb code 1e9c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp, PDB code: 1e9c:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:14.5 occ:1.00 O2B A:ADP302 2.0 9.6 0.5 O3G A:ANP303 2.1 17.8 0.5 O A:HOH2249 2.1 11.3 1.0 O A:HOH2255 2.1 7.8 0.5 OG A:SER20 2.1 10.0 1.0 O A:HOH2024 2.1 13.4 1.0 O2B A:ANP303 2.1 16.7 0.5 O A:HOH2248 2.2 10.1 1.0 CB A:SER20 3.1 8.6 1.0 PG A:ANP303 3.2 24.2 0.5 PB A:ANP303 3.2 16.5 0.5 PB A:ADP302 3.3 8.1 0.5 N3B A:ANP303 3.4 18.4 0.5 O3B A:ADP302 3.6 8.0 0.5 O2P A:TMP301 3.8 17.5 0.5 O1P A:TMP301 3.9 18.1 0.5 O1A A:ADP302 4.0 11.1 0.5 N A:SER20 4.0 10.6 1.0 O A:HOH2262 4.0 42.8 1.0 OD2 A:ASP96 4.1 12.5 1.0 O A:HOH2127 4.1 17.6 1.0 O A:HOH2256 4.1 27.4 0.5 O2G A:ANP303 4.1 25.2 0.5 CA A:SER20 4.1 9.2 1.0 O2A A:ANP303 4.2 13.1 0.5 P A:TMP301 4.2 17.5 0.5 O3A A:ADP302 4.3 9.5 0.5 O3A A:ANP303 4.3 16.6 0.5 O3P A:TMP301 4.3 20.9 0.5 O1B A:ADP302 4.3 7.8 0.5 O1G A:ANP303 4.3 26.2 0.5 O1P A:TMP301 4.3 16.8 0.5 OD1 A:ASP96 4.3 10.6 1.0 O2P A:TMP301 4.4 19.1 0.5 O1B A:ANP303 4.4 16.9 0.5 PA A:ADP302 4.6 9.7 0.5 P A:TMP301 4.6 20.3 0.5 CG A:ASP96 4.7 8.1 1.0 O A:HOH2260 4.8 33.1 1.0 PA A:ANP303 4.8 15.8 0.5 CB A:LYS19 4.9 11.9 1.0 CE A:LYS19 5.0 13.5 1.0

Magnesium binding site 2 out of 2 in the Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Mutant Human Thymidylate Kinase Complexed with Tmp and Appnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:21.4 occ:0.50 O A:HOH2057 2.1 26.8 1.0 O A:HOH2146 2.4 27.9 1.0 O A:HOH2142 2.5 21.7 1.0 OE1 A:GLN119 4.3 9.6 1.0 OD1 A:ASP115 4.5 22.0 1.0 CD A:GLN119 4.5 14.1 1.0 OD2 A:ASP115 4.6 24.1 1.0 O A:HOH2152 4.7 30.8 1.0 NE2 A:GLN119 4.7 10.6 1.0

N.Ostermann, A.Lavie, S.Padiyar, R.Brundiers, T.Veit, J.Reintein, R.S.Goody, M.Konrad, I.Schlichting. Potentiating Azt Activation: Structures of Wildtype and Mutant Human Thymidylate Kinase Suggest Reasons For the Mutants' Improved Kinetics with the Hiv Prodrug Metabolite Aztmp J.Mol.Biol. V. 304 43 2000.
ISSN: ISSN 0022-2836
PubMed: 11071809
DOI: 10.1006/JMBI.2000.4175