Nickel in PDB 2wwu: Crystal Structure of the Catalytic Domain of Phd Finger Protein 8

The structure of Crystal Structure of the Catalytic Domain of Phd Finger Protein 8, PDB code: 2wwu was solved by W.W.Yue, V.Hozjan, C.Cooper, A.Tumber, T.Krojer, J.Muniz, C.Allerston, E.Salah, M.A.Mcdonough, F.Von Delft, C.Arrowsmith, J.Weigelt, A.Edwards, C.Bountra, C.J.Schofield, K.L.Kavanagh, U.Oppermann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.76 / 2.15
Space group	I 21 3
Cell size a, b, c (Å), α, β, γ (°)	150.980, 150.980, 150.980, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.2

The binding sites of Nickel atom in the Crystal Structure of the Catalytic Domain of Phd Finger Protein 8 (pdb code 2wwu). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of the Catalytic Domain of Phd Finger Protein 8, PDB code: 2wwu:

Nickel binding site 1 out of 1 in the Crystal Structure of the Catalytic Domain of Phd Finger Protein 8


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the Catalytic Domain of Phd Finger Protein 8 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni1491 b:98.5 occ:1.00 NE2 A:HIS247 2.5 40.6 1.0 OD1 A:ASP249 2.6 55.6 1.0 NE2 A:HIS319 2.8 42.8 1.0 CE1 A:HIS247 3.1 40.7 1.0 OH A:TYR257 3.2 64.1 1.0 CG A:ASP249 3.6 59.5 1.0 CE1 A:HIS319 3.6 38.0 1.0 CD2 A:HIS319 3.7 42.5 1.0 CD2 A:HIS247 3.7 40.1 1.0 OD2 A:ASP249 3.9 74.3 1.0 CZ A:TYR257 4.2 66.2 1.0 CE2 A:TYR257 4.4 62.6 1.0 ND1 A:HIS247 4.4 44.4 1.0 CG A:HIS247 4.7 41.5 1.0 ND1 A:HIS319 4.7 43.7 1.0 O A:HOH2077 4.8 49.1 1.0 CG A:HIS319 4.8 43.7 1.0 CB A:ASP249 4.9 47.6 1.0

W.W.Yue, V.Hozjan, W.Ge, C.Loenarz, C.D.Cooper, C.J.Schofield, K.L.Kavanagh, U.Oppermann, M.A.Mcdonough. Crystal Structure of the PHF8 Jumonji Domain, An Nepsilon-Methyl Lysine Demethylase. Febs Lett. V. 584 825 2010.
ISSN: ISSN 1873-3468
PubMed: 20067792
DOI: 10.1016/J.FEBSLET.2009.12.055