Manganese in PDB 2d0c: Crystal Structure of Bst-Rnase Hiii in Complex with MN2+

All present enzymatic activity of Crystal Structure of Bst-Rnase Hiii in Complex with MN2+:
3.1.26.4;

The structure of Crystal Structure of Bst-Rnase Hiii in Complex with MN2+, PDB code: 2d0c was solved by H.Chon, H.Matsumura, Y.Koga, K.Takano, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.64 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.288, 109.771, 48.370, 90.00, 90.00, 90.00
R / Rfree (%)	20.9 / 27.4

The binding sites of Manganese atom in the Crystal Structure of Bst-Rnase Hiii in Complex with MN2+ (pdb code 2d0c). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Bst-Rnase Hiii in Complex with MN2+, PDB code: 2d0c:

Manganese binding site 1 out of 1 in the Crystal Structure of Bst-Rnase Hiii in Complex with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Bst-Rnase Hiii in Complex with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn501 b:39.7 occ:1.00 O A:HOH567 2.1 26.9 1.0 OD2 A:ASP202 2.2 42.1 1.0 OD1 A:ASP97 2.3 37.1 1.0 O A:HOH568 2.4 50.1 1.0 O A:HOH569 2.6 48.9 1.0 OE2 A:GLU98 2.7 40.6 1.0 O A:HOH572 3.2 39.0 1.0 CG A:ASP202 3.3 40.2 1.0 CG A:ASP97 3.3 40.1 1.0 CD A:GLU98 3.7 39.6 1.0 OD2 A:ASP97 3.7 44.0 1.0 CB A:ASP202 3.8 38.1 1.0 OE1 A:GLU98 3.9 36.7 1.0 O A:HOH524 4.0 41.1 1.0 O A:ASP202 4.1 37.8 1.0 OD1 A:ASP202 4.4 42.8 1.0 N A:GLU98 4.5 33.5 1.0 CB A:ASP97 4.6 37.7 1.0 O A:GLU98 4.6 31.3 1.0 CA A:ASP97 4.7 36.8 1.0 O A:HOH516 4.8 45.6 1.0 C A:ASP202 4.8 37.1 1.0 O A:GLU203 4.8 41.2 1.0 CA A:ASP202 4.9 37.0 1.0 O A:HOH605 5.0 47.6 1.0

H.Chon, H.Matsumura, Y.Koga, K.Takano, S.Kanaya. Crystal Structure and Structure-Based Mutational Analyses of Rnase Hiii From Bacillus Stearothermophilus: A New Type 2 Rnase H with Tbp-Like Substrate-Binding Domain at the N Terminus J.Mol.Biol. V. 356 165 2006.
ISSN: ISSN 0022-2836
PubMed: 16343535
DOI: 10.1016/J.JMB.2005.11.017