Manganese in PDB 1wse: Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+

All present enzymatic activity of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+:
3.1.26.4;

The structure of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+, PDB code: 1wse was solved by Y.Tsunaka, K.Takano, H.Matsumura, Y.Yamagata, S.Kanaya, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.30
Space group	P 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.041, 66.008, 79.485, 90.00, 90.00, 90.00
R / Rfree (%)	23 / 28.8

The binding sites of Manganese atom in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+ (pdb code 1wse). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+, PDB code: 1wse:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:43.2 occ:1.00 OD1 A:ASP10 2.4 34.4 1.0 OD1 A:ASP134 2.5 29.1 1.0 O A:HOH1021 2.6 33.8 1.0 OD2 A:ASP10 2.9 30.4 1.0 CG A:ASP10 3.0 28.4 1.0 CG A:ASP134 3.6 25.4 1.0 OD1 A:ASP70 3.9 54.4 1.0 CB A:ASP134 4.0 25.7 1.0 O A:GLY11 4.2 25.3 1.0 OD2 A:ASP70 4.2 53.0 1.0 NH2 A:ARG138 4.3 49.2 1.0 O A:HOH1048 4.3 45.0 1.0 CG A:ASP70 4.5 52.0 1.0 CA A:ASP134 4.5 23.2 1.0 CB A:ASP10 4.5 26.8 1.0 OD2 A:ASP134 4.7 28.4 1.0 CZ A:ARG138 4.9 48.4 1.0

Manganese binding site 2 out of 2 in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A*) with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn1002 b:64.9 occ:1.00 OD1 B:ASP10 2.4 38.3 1.0 OD1 B:ASP134 2.4 41.3 1.0 OD2 B:ASP10 2.7 36.4 1.0 CG B:ASP10 2.9 37.2 1.0 OD2 B:ASP70 3.4 55.3 1.0 CG B:ASP134 3.6 41.7 1.0 O B:GLY11 3.9 37.5 1.0 CB B:ASP134 4.1 38.1 1.0 CG B:ASP70 4.3 51.4 1.0 OD1 B:ASP70 4.4 55.7 1.0 CB B:ASP10 4.4 35.2 1.0 CA B:ASP134 4.6 36.3 1.0 O B:HOH1064 4.6 43.5 1.0 OD2 B:ASP134 4.6 42.9 1.0 NH2 B:ARG138 5.0 56.6 1.0

Y.Tsunaka, K.Takano, H.Matsumura, Y.Yamagata, S.Kanaya. Identification of Single Mn(2+) Binding Sites Required For Activation of the Mutant Proteins of E.Coli Rnase Hi at GLU48 and/or ASP134 By X-Ray Crystallography J.Mol.Biol. V. 345 1171 2005.
ISSN: ISSN 0022-2836
PubMed: 15644213
DOI: 10.1016/J.JMB.2004.11.007