Magnesium in PDB 7aul: Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg

Enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg

All present enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg:
3.6.1.52; 3.6.1.60;

Protein crystallography data

The structure of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg, PDB code: 7aul 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) 46.69 / 1.85
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.634, 61.634, 95.978, 90, 90, 120
R / Rfree (%) 25.9 / 28.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg (pdb code 7aul). 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 in Complex with 5-INSP7 in Presence of Mg, PDB code: 7aul:

Magnesium binding site 1 out of 1 in 7aul

Go back to Magnesium Binding Sites List in 7aul
Magnesium binding site 1 out of 1 in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with 5-INSP7 in Presence of Mg


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 in Complex with 5-INSP7 in Presence of Mg within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg203

b:63.2
occ:0.50
 O25 A:I7P201 1.8 88.7 0.5
O22 A:I7P201 1.9 57.1 0.5
O65 A:I7P201 2.2 72.4 0.5
OE1 A:GLU84 2.4 35.6 1.0
O43 A:I7P201 2.4 64.3 0.5
O A:LYS63 2.4 38.7 1.0
O44 A:I7P201 2.4 110.0 0.5
O A:HOH331 2.6 40.6 1.0
PA2 A:I7P201 2.9 55.2 0.5
O32 A:I7P201 2.9 58.8 0.5
PA5 A:I7P201 3.0 88.2 0.5
CD A:GLU84 3.4 33.0 1.0
PB5 A:I7P201 3.4 77.3 0.5
O45 A:I7P201 3.5 82.6 0.5
C A:LYS63 3.5 32.8 1.0
O15 A:I7P201 3.6 98.1 0.5
PA4 A:I7P201 3.6 110.4 0.5
PA3 A:I7P201 3.6 65.3 0.5
O14 A:I7P201 3.8 109.4 0.5
OE2 A:GLU84 3.8 32.6 1.0
CA A:GLY64 3.8 32.2 1.0
O13 A:I7P201 3.9 65.6 0.5
O12 A:I7P201 4.0 60.2 0.5
O42 A:I7P201 4.0 57.1 0.5
N A:GLY64 4.1 31.1 1.0
O34 A:I7P201 4.1 106.8 0.5
NZ A:LYS63 4.2 35.3 1.0
O33 A:I7P201 4.2 65.4 0.5
CG A:LYS63 4.2 35.8 1.0
O35 A:I7P201 4.3 89.3 0.5
O75 A:I7P201 4.3 77.5 0.5
NH2 A:ARG152 4.3 40.3 1.0
O55 A:I7P201 4.5 73.6 0.5
C5 A:I7P201 4.6 105.3 0.5
C2 A:I7P201 4.6 62.1 0.5
CA A:LYS63 4.7 32.4 1.0
CG A:GLU84 4.7 32.6 1.0
OE2 A:GLU80 4.7 40.9 1.0
N A:LYS63 4.7 30.8 1.0
C4 A:I7P201 4.8 106.3 0.5
O A:ACT202 4.8 52.2 1.0
O23 A:I7P201 4.9 60.5 0.5
O24 A:I7P201 4.9 107.2 0.5
C3 A:I7P201 4.9 62.4 0.5

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: Sun Jul 11 15:42:10 2021

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