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Magnesium in PDB 7auu: Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6

Enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6

All present enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6:
3.6.1.52; 3.6.1.60;

Protein crystallography data

The structure of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6, PDB code: 7auu was solved by M.A.Marquez-Monino, B.Gonzalez, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.54 / 2.45
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.12, 62.12, 92.472, 90, 90, 120
R / Rfree (%) 20.6 / 25.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6 (pdb code 7auu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6, PDB code: 7auu:

Magnesium binding site 1 out of 1 in 7auu

Go back to Magnesium Binding Sites List in 7auu
Magnesium binding site 1 out of 1 in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1-Nose Mutant in Complex with INSP6 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:96.0
occ:1.00
 O32 A:IHP201 1.9 133.1 1.0
OE1 A:GLU84 2.2 70.8 1.0
O A:HOH312 2.4 82.1 1.0
O A:HOH313 2.5 80.4 1.0
O A:LYS63 2.5 64.8 1.0
O23 A:IHP201 3.0 117.3 1.0
P2 A:IHP201 3.2 131.0 1.0
CD A:GLU84 3.3 68.5 1.0
C A:LYS63 3.6 62.2 1.0
CA A:GLY64 3.7 57.3 1.0
OE2 A:GLU84 3.7 66.9 1.0
O42 A:IHP201 3.7 125.4 1.0
O22 A:IHP201 3.8 124.1 1.0
N A:GLY64 4.1 58.2 1.0
P3 A:IHP201 4.1 123.2 1.0
O13 A:IHP201 4.2 120.6 1.0
OE2 A:GLU80 4.2 74.0 1.0
NH2 A:ARG132 4.3 76.1 1.0
O12 A:IHP201 4.4 133.3 1.0
CG A:GLU84 4.6 67.3 1.0
CD A:GLU80 4.6 71.2 1.0
O33 A:IHP201 4.7 119.4 1.0
OE1 A:GLU80 4.8 75.2 1.0
NZ A:LYS63 4.8 77.6 1.0
CA A:LYS63 4.8 63.3 1.0
N A:LYS63 4.9 61.6 1.0

Reference:

M.A.Marquez-Monino, R.Ortega-Garcia, M.L.Shipton, E.Franco-Echevarria, A.M.Riley, J.Sanz-Aparicio, B.V.L.Potter, B.Gonzalez. Multiple Substrate Recognition By Yeast Diadenosine and Diphosphoinositol Polyphosphate Phosphohydrolase Through Phosphate Clamping. Sci Adv V. 7 2021.
ISSN: ESSN 2375-2548
PubMed: 33893105
DOI: 10.1126/SCIADV.ABF6744
Page generated: Wed Oct 2 10:14:27 2024

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