Magnesium in PDB 3fzi: 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212

All present enzymatic activity of 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212:
3.1.11.2;

The structure of 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212, PDB code: 3fzi was solved by K.Lakomek, A.Dickmanns, R.Ficner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.51 / 1.90
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	56.040, 56.040, 161.320, 90.00, 90.00, 120.00
R / Rfree (%)	19.8 / 26.2

The binding sites of Magnesium atom in the 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212 (pdb code 3fzi). 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 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212, PDB code: 3fzi:

Magnesium binding site 1 out of 1 in the 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of 1.9 Angstrom Structure of the Thermophilic Exonuclease III Homologue MTH0212 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg266 b:45.6 occ:1.00 O A:HOH391 2.2 42.1 1.0 OD1 A:ASN12 2.3 26.0 1.0 O A:HOH334 2.4 20.5 1.0 OE2 A:GLU38 2.6 38.0 1.0 O A:HOH335 2.6 30.7 1.0 CD A:GLU38 3.0 35.0 1.0 CG A:ASN12 3.3 21.4 1.0 NZ A:LYS40 3.4 35.9 1.0 OE1 A:GLU38 3.4 39.5 1.0 CB A:ASN12 3.9 19.5 1.0 CG A:GLU38 4.0 29.1 1.0 CA A:ASN12 4.0 19.4 1.0 O A:HOH406 4.0 33.6 1.0 CE A:LYS40 4.3 29.8 1.0 ND2 A:ASN12 4.3 22.9 1.0 OD1 A:ASP247 4.4 27.0 1.0 OD2 A:ASP247 4.4 24.3 1.0 O A:HOH484 4.4 48.3 1.0 OD1 A:ASN10 4.7 16.9 1.0 CG A:ASP247 4.8 24.3 1.0 C A:ASN12 4.9 19.7 1.0 N A:ASN12 5.0 19.2 1.0 CB A:GLU38 5.0 22.0 1.0

K.Lakomek, A.Dickmanns, E.Ciirdaeva, L.Schomacher, R.Ficner. Crystal Structure Analysis of Dna Uridine Endonuclease MTH212 Bound to Dna J.Mol.Biol. V. 399 604 2010.
ISSN: ISSN 0022-2836
PubMed: 20434457
DOI: 10.1016/J.JMB.2010.04.044