Manganese in PDB 2fc0: Wrn Exonuclease, Mn Dgmp Complex

The structure of Wrn Exonuclease, Mn Dgmp Complex, PDB code: 2fc0 was solved by J.J.Perry, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.90 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	81.104, 81.104, 93.560, 90.00, 90.00, 120.00
R / Rfree (%)	22.3 / 23.8

The binding sites of Manganese atom in the Wrn Exonuclease, Mn Dgmp Complex (pdb code 2fc0). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Wrn Exonuclease, Mn Dgmp Complex, PDB code: 2fc0:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Wrn Exonuclease, Mn Dgmp Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Wrn Exonuclease, Mn Dgmp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn237 b:31.4 occ:1.00 OE2 A:GLU84 2.0 28.2 1.0 OD1 A:ASP82 2.0 29.3 1.0 OD2 A:ASP216 2.1 32.7 1.0 O A:HOH257 2.2 45.0 1.0 O A:HOH425 2.2 33.8 1.0 O A:HOH369 2.3 38.4 1.0 CG A:ASP216 3.0 29.8 1.0 CD A:GLU84 3.0 27.1 1.0 CG A:ASP82 3.1 28.4 1.0 OE1 A:GLU84 3.4 28.1 1.0 CB A:ASP216 3.5 25.8 1.0 OD2 A:ASP82 3.6 27.8 1.0 MN A:MN238 3.7 42.8 1.0 O A:HOH396 3.8 45.2 1.0 OD1 A:ASP216 4.0 31.0 1.0 O A:HOH248 4.0 48.1 1.0 O A:HOH427 4.2 36.4 1.0 NH2 A:ARG196 4.3 42.6 1.0 O A:MET83 4.3 26.7 1.0 CG A:GLU84 4.4 24.7 1.0 CB A:ASP82 4.4 27.8 1.0 NE2 A:GLN101 4.4 24.8 1.0 O A:HOH426 4.5 51.3 1.0

Manganese binding site 2 out of 2 in the Wrn Exonuclease, Mn Dgmp Complex


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Wrn Exonuclease, Mn Dgmp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn238 b:42.8 occ:1.00 OD2 A:ASP82 2.2 27.8 1.0 O A:HOH427 2.3 36.4 1.0 O A:HOH424 2.3 41.7 1.0 O A:HOH425 2.3 33.8 1.0 O A:HOH374 2.5 34.1 1.0 O A:HOH248 3.0 48.1 1.0 CG A:ASP82 3.2 28.4 1.0 OD1 A:ASP82 3.4 29.3 1.0 O A:HOH257 3.5 45.0 1.0 MN A:MN237 3.7 31.4 1.0 O A:MET83 3.9 26.7 1.0 O A:HOH272 4.4 37.9 1.0 OD2 A:ASP143 4.4 32.9 1.0 OD1 A:ASP143 4.4 33.1 1.0 CB A:ASP82 4.5 27.8 1.0 N A:MET83 4.5 24.8 1.0 O A:VAL138 4.6 33.9 1.0 O A:HOH260 4.8 43.1 1.0 O A:HOH308 4.8 66.3 1.0 OE2 A:GLU84 4.9 28.2 1.0 CA A:ASP82 4.9 27.1 1.0 CG A:ASP143 4.9 34.0 1.0 O A:HOH369 5.0 38.4 1.0 C A:MET83 5.0 25.7 1.0

J.J.Perry, S.M.Yannone, L.G.Holden, C.Hitomi, A.Asaithamby, S.Han, P.K.Cooper, D.J.Chen, J.A.Tainer. Wrn Exonuclease Structure and Molecular Mechanism Imply An Editing Role in Dna End Processing. Nat.Struct.Mol.Biol. V. 13 414 2006.
ISSN: ISSN 1545-9993
PubMed: 16622405
DOI: 10.1038/NSMB1088