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Nickel in PDB 7z2y: Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate

Enzymatic activity of Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate

All present enzymatic activity of Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate:
3.1.3.2; 3.1.3.26;

Protein crystallography data

The structure of Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate, PDB code: 7z2y 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) 41.15 / 1.86
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.554, 47.464, 65.445, 90, 100.69, 90
R / Rfree (%) 18.3 / 25.8

Nickel Binding Sites:

The binding sites of Nickel atom in the Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate (pdb code 7z2y). 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 T305E Mutant, Complex with Myo-Inositol Hexakissulfate, PDB code: 7z2y:

Nickel binding site 1 out of 1 in 7z2y

Go back to Nickel Binding Sites List in 7z2y
Nickel binding site 1 out of 1 in the Escherichia Coli Periplasmic Phytase Appa T305E Mutant, Complex with Myo-Inositol Hexakissulfate


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 T305E Mutant, Complex with Myo-Inositol Hexakissulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni503

b:24.1
occ:1.00
 O A:HOH603 2.1 51.3 1.0
OG1 A:THR327 2.1 14.2 1.0
OD2 A:ASP304 2.2 12.3 0.4
OD1 A:ASP325 2.2 5.8 1.0
NE2 A:HIS250 2.5 10.5 1.0
O A:THR327 2.9 9.4 1.0
O A:HOH684 3.0 13.7 1.0
CG A:ASP325 3.0 6.2 1.0
CG A:ASP304 3.1 11.7 0.4
OD2 A:ASP325 3.1 7.8 1.0
CD2 A:HIS250 3.2 11.7 1.0
CB A:THR327 3.2 11.2 1.0
OD1 A:ASP304 3.4 12.8 0.4
C A:THR327 3.4 8.3 1.0
N A:THR327 3.5 7.5 1.0
CA A:THR327 3.6 8.1 1.0
CE1 A:HIS250 3.6 11.1 1.0
OD2 A:ASP304 3.6 8.5 0.6
CB A:ASP304 3.9 9.8 0.6
NH1 A:ARG16 4.1 10.1 1.0
CG A:ASP304 4.1 7.7 0.6
CB A:ASP304 4.3 10.8 0.4
CG2 A:THR327 4.4 11.6 1.0
CG A:HIS250 4.4 11.1 1.0
CB A:ASP325 4.5 6.9 1.0
OE1 A:GLU219 4.5 7.6 1.0
N A:PRO328 4.5 7.4 1.0
ND1 A:HIS250 4.6 11.9 1.0
OD1 A:ASN251 4.7 8.3 1.0
CE1 A:PHE254 4.7 7.4 1.0
N A:ASN326 4.7 11.5 1.0
C A:ASN326 4.7 12.3 1.0
CD1 A:PHE254 4.7 8.0 1.0
CZ A:ARG16 4.8 10.0 1.0
C A:ASP325 4.9 10.5 1.0
CZ A:PHE254 4.9 8.4 1.0
OE2 A:GLU219 4.9 9.2 1.0
CD A:GLU219 4.9 7.6 1.0
CA A:ASP325 5.0 10.1 1.0
CA A:PRO328 5.0 6.3 1.0

Reference:

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
Page generated: Fri Apr 7 19:27:02 2023

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