Manganese in PDB 3buc: X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG

The structure of X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG, PDB code: 3buc was solved by C.-G.Yang, C.Yi, C.He, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.59
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	77.910, 77.910, 226.558, 90.00, 90.00, 120.00
R / Rfree (%)	24.8 / 28.7

The binding sites of Manganese atom in the X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG (pdb code 3buc). 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 X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG, PDB code: 3buc:

Manganese binding site 1 out of 1 in the X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of X-Ray Structure of Human ABH2 Bound to Dsdna with Mn(II) and 2KG within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1 b:42.1 occ:1.00 O A:HOH270 1.9 64.4 1.0 O1 A:AKG259 2.0 48.1 1.0 OD2 A:ASP173 2.0 50.1 1.0 NE2 A:HIS171 2.1 45.8 1.0 NE2 A:HIS236 2.2 45.4 1.0 O5 A:AKG259 2.4 45.1 1.0 C1 A:AKG259 2.8 47.4 1.0 CE1 A:HIS171 2.9 46.1 1.0 CG A:ASP173 3.0 49.5 1.0 C2 A:AKG259 3.0 46.7 1.0 CE1 A:HIS236 3.1 45.5 1.0 CD2 A:HIS236 3.2 45.9 1.0 CD2 A:HIS171 3.2 45.9 1.0 OD1 A:ASP173 3.3 50.6 1.0 O2 A:AKG259 4.0 48.3 1.0 ND1 A:HIS171 4.0 46.1 1.0 ND1 A:HIS236 4.2 45.7 1.0 CG A:HIS171 4.2 46.4 1.0 CG A:HIS236 4.3 45.9 1.0 N1 B:MA77 4.3 42.8 1.0 CB A:ASP173 4.4 49.0 1.0 NH2 A:ARG254 4.4 48.5 1.0 CN B:MA77 4.4 43.1 1.0 C2 B:MA77 4.5 43.4 1.0 C3 A:AKG259 4.5 45.7 1.0 C6 B:MA77 4.7 42.2 1.0 N A:ASP173 4.9 48.5 1.0

C.G.Yang, C.Yi, E.M.Duguid, C.T.Sullivan, X.Jian, P.A.Rice, C.He. Crystal Structures of Dna/Rna Repair Enzymes Alkb and ABH2 Bound to Dsdna. Nature V. 452 961 2008.
ISSN: ISSN 0028-0836
PubMed: 18432238
DOI: 10.1038/NATURE06889