Manganese in PDB 1wsg: Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A/D134N*) with MN2+

All present enzymatic activity of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A/D134N*) with MN2+:
3.1.26.4;

The structure of Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A/D134N*) with MN2+, PDB code: 1wsg 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 / 2.20
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	120.223, 79.879, 64.198, 90.00, 90.00, 90.00
R / Rfree (%)	22.1 / 29

The binding sites of Manganese atom in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A/D134N*) with MN2+ (pdb code 1wsg). 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/D134N*) with MN2+, PDB code: 1wsg:
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/D134N*) 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/D134N*) with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1001 b:64.9 occ:1.00 OD2 A:ASP70 2.4 44.2 1.0 OD1 A:ASP10 2.5 33.9 1.0 CE1 A:HIS124 2.7 72.5 1.0 CG A:ASP70 3.3 41.8 1.0 CG A:ASP10 3.4 28.5 1.0 ND1 A:HIS124 3.5 72.7 1.0 OD1 A:ASP70 3.5 42.0 1.0 OD2 A:ASP10 3.6 27.9 1.0 NE2 A:HIS124 3.6 72.2 1.0 OD1 A:ASN134 4.0 28.2 1.0 O A:GLY11 4.2 21.1 1.0 O A:HOH1048 4.3 41.8 1.0 CG A:HIS124 4.7 73.2 1.0 CB A:ASP70 4.7 37.3 1.0 CD2 A:HIS124 4.8 73.0 1.0 CG A:ASN134 4.8 28.0 1.0 CB A:ASP10 4.8 25.2 1.0 O A:HOH1077 4.8 35.9 1.0

Manganese binding site 2 out of 2 in the Co-Crystal Structure of E.Coli Rnase Hi Active Site Mutant (E48A/D134N*) 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/D134N*) with MN2+ within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn1002 b:54.1 occ:1.00 OD2 D:ASP10 2.3 37.0 1.0 O D:GLY11 2.3 21.3 1.0 CG D:ASP10 3.0 31.5 1.0 O D:HOH1042 3.1 24.8 1.0 OD1 D:ASP10 3.1 34.9 1.0 C D:GLY11 3.4 19.1 1.0 N D:GLY11 3.7 19.6 1.0 O D:HOH1101 3.8 46.0 1.0 CA D:GLY11 4.2 19.8 1.0 OD1 D:ASP70 4.2 36.5 1.0 OD2 D:ASP70 4.2 35.6 1.0 N D:SER12 4.3 20.8 1.0 OD1 D:ASN134 4.3 30.3 1.0 CB D:ASP10 4.3 26.1 1.0 OD1 D:ASN44 4.4 29.2 1.0 C D:ASP10 4.5 21.0 1.0 CA D:SER12 4.5 22.0 1.0 CG D:ASP70 4.6 32.8 1.0 CA D:ASP10 4.7 22.6 1.0 CB D:SER12 4.8 22.1 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