Magnesium in PDB 1hz1: Ribonuclease T1 V16A Mutant in Complex with MG2+

All present enzymatic activity of Ribonuclease T1 V16A Mutant in Complex with MG2+:
3.1.27.3;

The structure of Ribonuclease T1 V16A Mutant in Complex with MG2+, PDB code: 1hz1 was solved by J.De Swarte, S.De Vos, U.Langhorst, J.Steyaert, R.Loris, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	40.515, 47.289, 50.023, 90.00, 90.00, 90.00
R / Rfree (%)	19.6 / 21.4

The binding sites of Magnesium atom in the Ribonuclease T1 V16A Mutant in Complex with MG2+ (pdb code 1hz1). 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 Ribonuclease T1 V16A Mutant in Complex with MG2+, PDB code: 1hz1:

Magnesium binding site 1 out of 1 in the Ribonuclease T1 V16A Mutant in Complex with MG2+


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ribonuclease T1 V16A Mutant in Complex with MG2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg105 b:33.3 occ:1.00 O A:HOH226 2.4 32.8 1.0 O A:HOH256 2.4 43.0 1.0 OD2 A:ASP15 2.5 18.7 1.0 O A:HOH227 2.5 33.6 1.0 O A:HOH269 2.5 45.5 1.0 O A:HOH282 2.6 48.1 1.0 OD1 A:ASP15 2.7 17.8 1.0 CG A:ASP15 2.9 18.3 1.0 O A:HOH224 3.9 31.7 1.0 CB A:ASP15 4.3 16.9 1.0 O A:CYS10 4.6 17.6 1.0 O A:HOH215 4.6 24.9 1.0 OG A:SER12 4.6 18.6 1.0 O A:HOH277 4.8 47.0 1.0 N A:SER12 5.0 17.7 1.0

J.Deswarte, S.De Vos, U.Langhorst, J.Steyaert, R.Loris. The Contribution of Metal Ions to the Conformational Stability of Ribonuclease T1: Crystal Versus Solution. Eur.J.Biochem. V. 268 3993 2001.
ISSN: ISSN 0014-2956
PubMed: 11453993
DOI: 10.1046/J.1432-1327.2001.02310.X