Manganese in PDB 2xdv: Crystal Structure of the Catalytic Domain of FLJ14393

The structure of Crystal Structure of the Catalytic Domain of FLJ14393, PDB code: 2xdv was solved by T.Krojer, J.R.C.Muniz, S.S.Ng, E.Pilka, K.Guo, A.C.W.Pike, P.Filippakopoulos, S.Knapp, K.L.Kavanagh, O.Gileadi, G.Bunkoczi, W.W.Yue, F.Niesen, F.Sobott, O.Fedorov, P.Savitsky, G.Kochan, M.Daniel, F.Vondelft, C.H.Arrowsmith, A.M.Edwards, J.Weigelt, C.Bountra, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.28 / 2.57
Space group	P 43 3 2
Cell size a, b, c (Å), α, β, γ (°)	185.180, 185.180, 185.180, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.9

The structure of Crystal Structure of the Catalytic Domain of FLJ14393 also contains other interesting chemical elements:

Cadmium	(Cd)	3 atoms
Nickel	(Ni)	6 atoms

The binding sites of Manganese atom in the Crystal Structure of the Catalytic Domain of FLJ14393 (pdb code 2xdv). 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 Crystal Structure of the Catalytic Domain of FLJ14393, PDB code: 2xdv:

Manganese binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of FLJ14393


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 the Catalytic Domain of FLJ14393 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn1472 b:0.1 occ:0.50 OD2 A:ASP69 2.7 0.4 1.0 OD1 A:ASP69 3.1 0.4 1.0 CG A:ASP69 3.3 99.5 1.0 O A:ASP69 4.3 80.5 1.0 CB A:ASP69 4.7 77.0 1.0

R.Chowdhury, R.Sekirnik, N.C.Brissett, T.Krojer, C.H.Ho, S.S.Ng, I.J.Clifton, W.Ge, N.J.Kershaw, G.C.Fox, J.R.C.Muniz, M.Vollmar, C.Phillips, E.S.Pilka, K.L.Kavanagh, F.Von Delft, U.Oppermann, M.A.Mcdonough, A.J.Doherty, C.J.Schofield. Ribosomal Oxygenases Are Structurally Conserved From Prokaryotes to Humans. Nature V. 510 422 2014.
ISSN: ESSN 1476-4687
PubMed: 24814345
DOI: 10.1038/NATURE13263