Magnesium in PDB 2jcs: Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound

All present enzymatic activity of Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound:
2.7.1.145;

The structure of Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound, PDB code: 2jcs was solved by L.Egeblad-Welin, Y.Sonntag, H.Eklund, B.Munch-Petersen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.28 / 2.50
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	33.523, 119.467, 68.900, 90.00, 92.42, 90.00
R / Rfree (%)	23.2 / 24.2

The binding sites of Magnesium atom in the Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound (pdb code 2jcs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound, PDB code: 2jcs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1211 b:35.3 occ:1.00 O1B A:TTP1210 1.8 26.3 1.0 O3G A:TTP1210 2.0 28.0 1.0 OG1 A:THR34 2.1 44.1 1.0 O A:HOH2004 2.2 29.4 1.0 OE2 A:GLU104 2.3 34.5 1.0 OD1 A:ASP52 2.3 34.8 1.0 PB A:TTP1210 3.0 25.8 1.0 PG A:TTP1210 3.1 28.3 1.0 O3B A:TTP1210 3.1 27.0 1.0 CD A:GLU104 3.4 34.3 1.0 CB A:THR34 3.4 44.1 1.0 CG A:ASP52 3.4 34.7 1.0 OE1 A:GLU104 3.7 34.6 1.0 O1G A:TTP1210 3.7 28.3 1.0 OD2 A:ASP52 3.8 35.2 1.0 O3A A:TTP1210 3.8 25.3 1.0 N A:THR34 3.9 43.5 1.0 NH2 A:ARG169 4.1 33.2 1.0 O A:HOH2070 4.2 16.5 1.0 O2B A:TTP1210 4.2 25.4 1.0 CA A:THR34 4.3 44.2 1.0 O A:HOH2005 4.3 26.7 1.0 O2G A:TTP1210 4.3 28.2 1.0 CG2 A:THR34 4.4 44.1 1.0 NH1 A:ARG167 4.5 34.0 1.0 CB A:ASP52 4.7 34.5 1.0 CG A:GLU104 4.7 34.3 1.0 CB A:LYS33 4.7 42.3 1.0 CA A:ASP52 4.8 34.5 1.0 O A:HOH2053 4.8 26.8 1.0 C A:LYS33 4.9 42.9 1.0

Magnesium binding site 2 out of 2 in the Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Active Site Mutant of Dnk From D. Melanogaster with Dttp Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1211 b:37.2 occ:1.00 O1B B:TTP1210 1.7 25.7 1.0 O3G B:TTP1210 2.0 27.2 1.0 OG1 B:THR34 2.1 44.2 1.0 OD1 B:ASP52 2.3 34.8 1.0 OE2 B:GLU104 2.3 34.5 1.0 PB B:TTP1210 3.0 25.1 1.0 PG B:TTP1210 3.2 27.3 1.0 O3B B:TTP1210 3.3 26.2 1.0 CD B:GLU104 3.3 34.3 1.0 CB B:THR34 3.3 44.1 1.0 CG B:ASP52 3.4 34.7 1.0 OE1 B:GLU104 3.6 34.6 1.0 OD2 B:ASP52 3.7 35.1 1.0 O1G B:TTP1210 3.8 26.6 1.0 O3A B:TTP1210 3.8 25.3 1.0 N B:THR34 3.9 43.5 1.0 O B:HOH2071 4.0 32.7 1.0 O B:HOH2072 4.1 21.2 1.0 NH2 B:ARG169 4.1 33.2 1.0 O2B B:TTP1210 4.2 25.4 1.0 CA B:THR34 4.2 44.2 1.0 CG2 B:THR34 4.3 44.1 1.0 O2G B:TTP1210 4.4 27.3 1.0 NH1 B:ARG167 4.6 34.0 1.0 CB B:ASP52 4.6 34.5 1.0 CG B:GLU104 4.7 34.3 1.0 CB B:LYS33 4.7 42.3 1.0 CA B:ASP52 4.7 34.5 1.0 O B:HOH2059 4.7 33.9 1.0 C B:LYS33 4.9 42.9 1.0

L.Egeblad-Welin, Y.Sonntag, H.Eklund, B.Munch-Petersen. Functional Studies of Active-Site Mutants From Drosophila Melanogaster Deoxyribonucleoside Kinase. Investigations of the Putative Catalytic Glutamate- Arginine Pair and of Residues Responsible For Substrate Specificity. Febs J. V. 274 1542 2007.
ISSN: ISSN 1742-464X
PubMed: 17302737
DOI: 10.1111/J.1742-4658.2007.05701.X