Manganese in PDB 1s8e: Crystal Structure of MRE11-3

The structure of Crystal Structure of MRE11-3, PDB code: 1s8e was solved by K.P.Hopfner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	12.00 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.960, 88.570, 144.990, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / 27.8

The binding sites of Manganese atom in the Crystal Structure of MRE11-3 (pdb code 1s8e). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 4 binding sites of Manganese where determined in the Crystal Structure of MRE11-3, PDB code: 1s8e:
Jump to Manganese binding site number: 1; 2; 3; 4;

Manganese binding site 1 out of 4 in the Crystal Structure of MRE11-3


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 MRE11-3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn401 b:42.9 occ:1.00 OD1 A:ASN84 2.3 51.4 1.0 OD1 A:ASP49 2.3 31.5 1.0 O A:HOH630 2.3 34.7 1.0 NE2 A:HIS173 2.4 45.5 1.0 ND1 A:HIS206 2.4 53.8 1.0 O A:HOH602 2.7 41.6 1.0 CE1 A:HIS206 3.1 53.0 1.0 CG A:ASP49 3.2 35.3 1.0 CG A:ASN84 3.3 53.7 1.0 CE1 A:HIS173 3.3 47.5 1.0 MN A:MN402 3.3 44.3 1.0 CD2 A:HIS173 3.4 43.1 1.0 OD2 A:ASP49 3.4 35.7 1.0 CG A:HIS206 3.6 53.1 1.0 ND2 A:ASN84 3.7 52.6 1.0 OD1 A:ASP8 4.0 41.5 1.0 CA A:HIS206 4.0 50.6 1.0 CB A:HIS206 4.1 51.5 1.0 NE2 A:HIS206 4.4 55.7 1.0 O A:HIS206 4.4 53.6 1.0 CB A:ASP49 4.4 34.0 1.0 ND1 A:HIS173 4.4 46.5 1.0 N A:ASN84 4.5 48.6 1.0 CG A:HIS173 4.5 44.4 1.0 CD2 A:HIS206 4.6 53.5 1.0 CB A:ASN84 4.6 51.0 1.0 C A:HIS206 4.7 51.3 1.0 N A:HIS206 5.0 46.9 1.0

Manganese binding site 2 out of 4 in the Crystal Structure of MRE11-3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of MRE11-3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn402 b:44.3 occ:1.00 OD1 A:ASP8 2.1 41.5 1.0 OD1 A:ASP49 2.2 31.5 1.0 NE2 A:HIS10 2.3 38.4 1.0 O A:HOH630 2.3 34.7 1.0 NE2 A:HIS208 2.4 46.7 1.0 CE1 A:HIS10 2.9 38.4 1.0 O A:HOH602 2.9 41.6 1.0 CG A:ASP8 3.2 42.1 1.0 CG A:ASP49 3.2 35.3 1.0 MN A:MN401 3.3 42.9 1.0 CE1 A:HIS208 3.4 45.7 1.0 CD2 A:HIS208 3.4 47.8 1.0 CD2 A:HIS10 3.5 37.8 1.0 CB A:ASP49 3.6 34.0 1.0 CB A:ASP8 3.7 36.9 1.0 ND1 A:HIS10 4.1 41.0 1.0 OD2 A:ASP8 4.2 39.7 1.0 O A:HIS206 4.2 53.6 1.0 CA A:ASP8 4.3 37.5 1.0 OD2 A:ASP49 4.3 35.7 1.0 CE1 A:HIS173 4.5 47.5 1.0 CG A:HIS10 4.5 39.1 1.0 ND1 A:HIS208 4.5 47.7 1.0 NE2 A:HIS173 4.5 45.5 1.0 CG A:HIS208 4.6 46.5 1.0 CA A:HIS206 4.7 50.6 1.0 C A:HIS206 4.8 51.3 1.0 ND1 A:HIS206 5.0 53.8 1.0

Manganese binding site 3 out of 4 in the Crystal Structure of MRE11-3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of MRE11-3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn403 b:41.5 occ:1.00 OD2 B:ASP49 2.1 37.5 1.0 OD1 B:ASP8 2.2 39.1 1.0 NE2 B:HIS10 2.3 42.5 1.0 NE2 B:HIS208 2.3 35.5 1.0 O B:HOH605 2.4 35.6 1.0 CE1 B:HIS10 3.0 37.7 1.0 CE1 B:HIS208 3.1 39.1 1.0 CG B:ASP8 3.2 37.9 1.0 CG B:ASP49 3.2 40.7 1.0 O B:HOH601 3.3 37.8 1.0 MN B:MN404 3.3 42.1 1.0 CD2 B:HIS208 3.4 38.7 1.0 CD2 B:HIS10 3.5 38.2 1.0 CB B:ASP49 3.7 36.9 1.0 CB B:ASP8 3.7 31.9 1.0 OD2 B:ASP8 4.2 36.0 1.0 ND1 B:HIS10 4.2 38.9 1.0 CA B:ASP8 4.3 35.6 1.0 ND1 B:HIS208 4.3 38.4 1.0 OD1 B:ASP49 4.3 40.1 1.0 O B:HIS206 4.4 41.2 1.0 CE1 B:HIS173 4.4 36.0 1.0 CG B:HIS208 4.5 37.6 1.0 CG B:HIS10 4.5 39.2 1.0 NE2 B:HIS173 4.5 36.2 1.0 CA B:HIS206 4.8 43.6 1.0 C B:HIS206 4.9 41.3 1.0 CD2 B:HIS206 5.0 50.7 1.0

Manganese binding site 4 out of 4 in the Crystal Structure of MRE11-3


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of MRE11-3 within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn404 b:42.1 occ:1.00 O B:HOH605 2.2 35.6 1.0 NE2 B:HIS173 2.3 36.2 1.0 OD1 B:ASN84 2.3 46.2 1.0 CD2 B:HIS206 2.4 50.7 1.0 OD2 B:ASP49 2.4 37.5 1.0 O B:HOH601 2.5 37.8 1.0 NE2 B:HIS206 3.1 52.1 1.0 CE1 B:HIS173 3.1 36.0 1.0 CG B:ASP49 3.1 40.7 1.0 CG B:ASN84 3.2 45.8 1.0 OD1 B:ASP49 3.3 40.1 1.0 MN B:MN403 3.3 41.5 1.0 CD2 B:HIS173 3.3 38.1 1.0 ND2 B:ASN84 3.4 40.6 1.0 CG B:HIS206 3.5 51.0 1.0 OD1 B:ASP8 4.0 39.1 1.0 CA B:HIS206 4.1 43.6 1.0 CB B:HIS206 4.2 47.1 1.0 ND1 B:HIS173 4.3 37.3 1.0 CE1 B:HIS206 4.3 54.4 1.0 CG B:HIS173 4.4 38.4 1.0 CB B:ASP49 4.4 36.9 1.0 O B:HIS206 4.5 41.2 1.0 ND1 B:HIS206 4.5 52.7 1.0 N B:ASN84 4.6 46.4 1.0 CB B:ASN84 4.6 46.0 1.0 C B:HIS206 4.8 41.3 1.0

L.M.Arthur, K.Gustausson, K.P.Hopfner, C.T.Carson, T.H.Stracker, A.Karcher, D.Felton, M.D.Weitzman, J.A.Tainer, J.P.Carney. Structural and Functional Analysis of MRE11-3 Nucleic Acids Res. V. 32 1886 2004.
ISSN: ISSN 0305-1048
PubMed: 15047855
DOI: 10.1093/NAR/GKH343