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Potassium in PDB 7z3v: Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate

Enzymatic activity of Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate

All present enzymatic activity of Escherichia Coli Periplasmic Phytase Appa D304E 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 D304E Mutant, Complex with Myo-Inositol Hexakissulfate, PDB code: 7z3v 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) 65.28 / 2.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 63.712, 44.35, 66.559, 90, 101.27, 90
R / Rfree (%) 19.5 / 27.1

Potassium Binding Sites:

The binding sites of Potassium atom in the Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate (pdb code 7z3v). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate, PDB code: 7z3v:

Potassium binding site 1 out of 1 in 7z3v

Go back to Potassium Binding Sites List in 7z3v
Potassium binding site 1 out of 1 in the Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Escherichia Coli Periplasmic Phytase Appa D304E Mutant, Complex with Myo-Inositol Hexakissulfate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K503

b:23.0
occ:1.00
O12 A:IHS502 2.7 27.9 0.9
O13 A:IHS502 2.8 25.8 0.9
O4 A:IHS502 3.1 18.1 0.9
O1 A:IHS502 3.1 23.1 0.9
C2 A:IHS502 3.2 23.8 0.9
O43 A:IHS502 3.4 17.1 0.9
S1 A:IHS502 3.5 28.9 0.9
C3 A:IHS502 3.5 25.6 0.9
O42 A:IHS502 3.6 25.2 0.9
O3 A:IHS502 3.6 22.4 0.9
C1 A:IHS502 3.7 24.5 0.9
H3 A:IHS502 3.8 30.8 0.9
S3 A:IHS502 3.8 21.8 0.9
S2 A:IHS502 3.8 23.8 0.9
H1 A:IHS502 4.0 29.4 0.9
H2 A:IHS502 4.1 28.6 0.9
NE2 A:GLN27 4.2 22.9 1.0
O22 A:IHS502 4.6 23.8 0.9
O23 A:IHS502 4.7 20.4 0.9
O32 A:IHS502 4.8 21.5 0.9
O15 A:IHS502 4.8 27.2 0.9
O33 A:IHS502 4.8 16.2 0.9
O2 A:IHS502 4.9 25.4 0.9
C4 A:IHS502 4.9 26.8 0.9

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: Mon Aug 12 21:45:06 2024

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