Nickel in PDB 9gle: Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S

All present enzymatic activity of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S:
1.14.11.66; 1.14.11.69;

The structure of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S, PDB code: 9gle was solved by M.Fairhead, C.Strain-Damerell, M.Ye, S.R.Mackinnon, D.Pinkas, E.M.Maclean, L.Koekemoer, D.Damerell, T.Krojer, C.H.Arrowsmith, A.Edwards, C.Bountra, W.Yue, N.Burgess-Brown, B.Marsden, F.Von Delft, Structural Genomicsconsortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.45 / 1.88
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	117.7, 90.78, 90.67, 90, 107.19, 90
R / Rfree (%)	18.5 / 22.2

The structure of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Nickel atom in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S (pdb code 9gle). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S, PDB code: 9gle:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni401 b:31.8 occ:1.00 OE2 A:GLU191 2.2 29.4 1.0 NE2 A:HIS189 2.2 30.2 1.0 NE2 A:HIS277 2.2 20.8 1.0 O A:HOH571 2.2 26.8 1.0 O A:HOH604 2.2 28.4 1.0 O A:HOH692 2.2 30.3 1.0 CE1 A:HIS277 3.0 25.1 1.0 CE1 A:HIS189 3.1 34.0 1.0 CD A:GLU191 3.1 29.0 1.0 HE1 A:HIS277 3.2 24.2 1.0 CD2 A:HIS189 3.2 30.4 1.0 CD2 A:HIS277 3.2 25.5 1.0 HE1 A:HIS189 3.3 31.3 1.0 HD2 A:HIS189 3.4 30.4 1.0 HD2 A:HIS277 3.4 23.5 1.0 OE1 A:GLU191 3.5 24.2 1.0 HG21 A:THR271 4.0 25.4 1.0 HZ1 A:LYS242 4.2 52.1 1.0 ND1 A:HIS277 4.2 25.7 1.0 O A:HOH717 4.2 52.8 1.0 ND1 A:HIS189 4.2 27.1 1.0 CG A:HIS277 4.3 21.7 1.0 CG A:HIS189 4.3 31.1 1.0 O A:HOH682 4.3 38.8 1.0 HZ3 A:LYS242 4.3 52.2 1.0 OG A:SER197 4.4 29.4 1.0 HG2 A:GLU191 4.4 27.5 1.0 CG A:GLU191 4.4 26.3 1.0 O A:HOH721 4.4 38.4 1.0 O2 A:EDO409 4.4 54.9 1.0 HZ3 A:TRP209 4.5 22.1 1.0 HA A:GLU191 4.6 26.1 1.0 NZ A:LYS242 4.7 54.6 1.0 HD2 A:PHE186 4.9 27.9 1.0 CG2 A:THR271 4.9 25.7 1.0 HB3 A:SER197 4.9 24.9 1.0 HG3 A:GLU191 4.9 27.5 1.0 OG1 A:THR271 4.9 25.3 1.0

Nickel binding site 2 out of 2 in the Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Jumonji Domain-Containing Protein 2A with Crystallization Epitope Mutations A91T:T93S within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni401 b:31.1 occ:1.00 OE1 B:GLU191 2.1 27.5 1.0 O B:HOH545 2.1 27.6 1.0 O B:HOH589 2.1 27.3 1.0 NE2 B:HIS277 2.2 27.1 1.0 O B:HOH644 2.2 30.9 1.0 NE2 B:HIS189 2.2 29.4 1.0 CE1 B:HIS277 3.1 28.2 1.0 CD B:GLU191 3.1 26.9 1.0 CE1 B:HIS189 3.2 32.6 1.0 CD2 B:HIS189 3.2 34.5 1.0 CD2 B:HIS277 3.2 27.1 1.0 HE1 B:HIS277 3.2 27.6 1.0 HE1 B:HIS189 3.3 31.6 1.0 HD2 B:HIS189 3.4 31.3 1.0 HD2 B:HIS277 3.4 27.2 1.0 OE2 B:GLU191 3.6 26.7 1.0 HG21 B:THR271 4.0 24.7 1.0 O B:HOH668 4.1 44.8 1.0 HZ3 B:LYS242 4.2 58.8 1.0 HZ1 B:LYS242 4.2 58.7 1.0 ND1 B:HIS277 4.3 26.6 1.0 ND1 B:HIS189 4.3 32.0 1.0 OG B:SER197 4.3 29.2 1.0 CG B:HIS189 4.3 26.5 1.0 HG2 B:GLU191 4.3 26.1 1.0 CG B:HIS277 4.3 27.6 1.0 HZ3 B:TRP209 4.4 29.8 1.0 CG B:GLU191 4.4 25.0 1.0 NZ B:LYS242 4.6 62.0 1.0 HA B:GLU191 4.7 26.8 1.0 HG3 B:GLU191 4.9 26.1 1.0 CG2 B:THR271 4.9 25.3 1.0 HD2 B:PHE186 4.9 31.3 1.0 HG22 B:THR271 5.0 24.6 1.0 HB3 B:SER197 5.0 26.0 1.0

M.Fairhead, C.Strain-Damerell, M.Ye, S.R.Mackinnon, D.Pinkas, E.M.Maclean, L.Koekemoer, D.Damerell, T.Krojer, W.Yue, N.Burgess-Brown, B.Marsden, F.Von Delft. A Fast, Parallel Method For Efficiently Exploring Crystallization Behaviour of Large Numbers of Protein Variants To Be Published.