Magnesium in PDB 2we3: Ebv Dutpase Inactive Mutant Deleted of Motif V

All present enzymatic activity of Ebv Dutpase Inactive Mutant Deleted of Motif V:
3.6.1.23;

The structure of Ebv Dutpase Inactive Mutant Deleted of Motif V, PDB code: 2we3 was solved by L.Freeman, M.Buisson, N.Tarbouriech, W.P.Burmeister, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	51.64 / 2.00
Space group	I 4
Cell size a, b, c (Å), α, β, γ (°)	103.238, 103.238, 47.697, 90.00, 90.00, 90.00
R / Rfree (%)	21.2 / 27.2

The binding sites of Magnesium atom in the Ebv Dutpase Inactive Mutant Deleted of Motif V (pdb code 2we3). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Ebv Dutpase Inactive Mutant Deleted of Motif V, PDB code: 2we3:

Magnesium binding site 1 out of 1 in the Ebv Dutpase Inactive Mutant Deleted of Motif V


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ebv Dutpase Inactive Mutant Deleted of Motif V within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1258 b:25.9 occ:1.00 O2A A:DUT1257 2.0 22.4 1.0 O2G A:DUT1257 2.0 23.6 1.0 O2B A:DUT1257 2.1 21.1 1.0 O A:HOH2048 2.1 20.9 1.0 O A:HOH2046 2.1 27.6 1.0 O A:HOH2082 2.2 24.1 1.0 PB A:DUT1257 3.1 20.8 1.0 PG A:DUT1257 3.1 26.4 1.0 PA A:DUT1257 3.2 22.0 1.0 O3A A:DUT1257 3.4 22.7 1.0 O3B A:DUT1257 3.5 20.8 1.0 O1G A:DUT1257 3.7 24.1 1.0 O A:HOH2078 4.1 23.6 1.0 OD2 A:ASP135 4.2 30.7 1.0 OD1 A:ASP135 4.2 31.3 1.0 NE A:ARG171 4.2 22.6 1.0 O5' A:DUT1257 4.2 26.4 1.0 O1A A:DUT1257 4.2 25.4 1.0 C5' A:DUT1257 4.3 23.3 1.0 O A:HOH2028 4.3 24.3 1.0 O3G A:DUT1257 4.4 20.4 1.0 O1B A:DUT1257 4.5 21.5 1.0 NH2 A:ARG171 4.6 22.6 1.0 NE2 A:GLN213 4.6 24.2 1.0 OD2 A:ASP76 4.6 34.1 1.0 CG A:ASP135 4.6 28.8 1.0 CZ A:ARG171 4.9 26.8 1.0 OD2 A:ASP131 4.9 45.3 1.0 OE1 A:GLN213 4.9 27.7 1.0 CG A:ARG171 5.0 22.9 1.0

L.Freeman, M.Buisson, N.Tarbouriech, A.Van Der Heyden, P.Labbe, W.P.Burmeister. The Flexible Motif V of Epstein-Barr Virus Deoxyuridine 5'-Triphosphate Pyrophosphatase Is Essential For Catalysis. J.Biol.Chem. V. 284 25280 2009.
ISSN: ISSN 0021-9258
PubMed: 19586911
DOI: 10.1074/JBC.M109.019315