Magnesium in PDB 3tpn: Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate

All present enzymatic activity of Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate:
3.6.1.23;

The structure of Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate, PDB code: 3tpn was solved by V.Nemeth, O.Barabas, G.B.Vertessy, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.88 / 1.65
Space group	P 63
Cell size a, b, c (Å), α, β, γ (°)	60.333, 60.333, 64.519, 90.00, 90.00, 120.00
R / Rfree (%)	15.7 / 18.2

The binding sites of Magnesium atom in the Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate (pdb code 3tpn). 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 Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate, PDB code: 3tpn:

Magnesium binding site 1 out of 1 in the Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of M-Pmv Dutpase Complexed with Dupnpp, Substrate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg999 b:16.4 occ:1.00 O2A A:DUP777 1.9 17.3 1.0 O1G A:DUP777 2.0 22.0 1.0 O2B A:DUP777 2.1 17.5 1.0 O A:HOH241 2.1 15.5 1.0 O A:HOH235 2.2 15.1 1.0 PB A:DUP777 3.1 18.9 1.0 PG A:DUP777 3.2 23.8 1.0 PA A:DUP777 3.2 16.0 1.0 O3B A:DUP777 3.4 21.6 1.0 N3A A:DUP777 3.5 13.0 1.0 O2G A:DUP777 3.7 22.8 1.0 O A:HOH177 3.8 23.2 1.0 O A:HOH155 4.2 15.7 1.0 O1A A:DUP777 4.2 17.7 1.0 O5' A:DUP777 4.3 17.8 1.0 O3G A:DUP777 4.4 24.2 1.0 O A:HOH252 4.5 40.6 1.0 C5' A:DUP777 4.5 15.6 1.0 O1B A:DUP777 4.5 20.0 1.0

O.Barabas, V.Nemeth, A.Bodor, A.Perczel, E.Rosta, Z.Kele, I.Zagyva, Z.Szabadka, V.I.Grolmusz, M.Wilmanns, B.G.Vertessy. Structural Snapshots of Enzyme-Catalysed Phosphate Ester Hydrolysis Directly Visualize in-Line Attack and Inversion To Be Published.