Nickel in PDB 7z32: Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate

All present enzymatic activity of Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate:
3.1.3.2; 3.1.3.26;

The structure of Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate, PDB code: 7z32 was solved by I.M.Acquistapace, C.A.Brearley, A.M.Hemmings, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.54 / 1.85
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.75, 47.96, 65.97, 90, 101.08, 90
R / Rfree (%)	16.3 / 22.4

The binding sites of Nickel atom in the Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate (pdb code 7z32). 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 Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate, PDB code: 7z32:

Nickel binding site 1 out of 1 in the Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Escherichia Coli Periplasmic Phytase Appa D304A Mutant, Phosphohistidine Intermediate within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni501 b:23.1 occ:1.00 OD1 A:ASP156 2.1 17.7 1.0 O A:HOH657 2.2 15.2 1.0 NE2 A:HIS160 2.2 21.3 1.0 O A:HOH764 2.3 23.3 1.0 O A:HOH882 2.4 21.6 1.0 O A:HOH918 2.5 25.6 1.0 CG A:ASP156 2.9 17.6 1.0 CD2 A:HIS160 3.1 18.0 1.0 OD2 A:ASP156 3.1 19.9 1.0 CE1 A:HIS160 3.3 19.9 1.0 O A:GLY151 4.2 15.9 1.0 CG A:HIS160 4.3 18.2 1.0 O A:HOH777 4.3 23.3 1.0 ND1 A:HIS160 4.3 19.1 1.0 CB A:ASP156 4.4 18.2 1.0 CA A:GLY151 4.4 16.2 1.0 O A:HOH978 4.4 39.0 1.0 C A:GLY151 4.8 15.7 1.0 O A:ASP156 4.9 16.2 1.0

I.M.Acquistapace, E.J.Thompson, I.Kuhn, M.R.Bedford, C.A.Brearley, A.M.Hemmings. Insights to the Structural Basis For the Stereospecificity of the Escherichia Coli Phytase, Appa. Int J Mol Sci V. 23 2022.
ISSN: ESSN 1422-0067
PubMed: 35683026
DOI: 10.3390/IJMS23116346