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Magnesium in PDB 7auj: Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7

Enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7

All present enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7:
3.6.1.52; 3.6.1.60;

Protein crystallography data

The structure of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7, PDB code: 7auj 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) 46.90 / 2.10
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.893, 61.893, 96.513, 90, 90, 120
R / Rfree (%) 22.5 / 26.5

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7 (pdb code 7auj). 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 Mutation E80Q in Complex with 1-INSP7, PDB code: 7auj:

Magnesium binding site 1 out of 1 in 7auj

Go back to Magnesium Binding Sites List in 7auj
Magnesium binding site 1 out of 1 in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 Mutation E80Q in Complex with 1-INSP7


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 Mutation E80Q in Complex with 1-INSP7 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg202

b:71.1
occ:1.00
 O A:HOH327 2.2 43.5 1.0
OE1 A:GLU84 2.5 50.0 1.0
O47 A:O81201 2.7 97.4 1.0
O A:LYS63 2.9 50.8 1.0
O36 A:O81201 2.9 91.9 1.0
O37 A:O81201 3.2 97.9 1.0
CD A:GLU84 3.4 48.8 1.0
P7 A:O81201 3.4 97.0 1.0
OE2 A:GLU84 3.5 47.7 1.0
P6 A:O81201 3.6 91.2 1.0
NZ A:LYS63 3.6 54.7 1.0
O16 A:O81201 3.6 91.6 1.0
O46 A:O81201 3.7 89.2 1.0
NH2 A:ARG152 3.9 61.1 1.0
C A:LYS63 3.9 49.4 1.0
CG A:LYS63 4.1 51.2 1.0
O27 A:O81201 4.4 96.1 1.0
O A:HOH328 4.4 55.8 1.0
CA A:GLY64 4.5 47.9 1.0
CE A:LYS63 4.6 53.4 1.0
N A:GLY64 4.6 48.6 1.0
CZ A:ARG152 4.6 61.1 1.0
NE2 A:GLN80 4.6 53.7 1.0
NH1 A:ARG152 4.7 61.4 1.0
N A:LYS63 4.7 47.1 1.0
CG A:GLU84 4.7 48.2 1.0
CA A:LYS63 4.8 48.5 1.0
C6 A:O81201 4.9 93.0 1.0
O41 A:O81201 5.0 97.7 1.0
CD A:LYS63 5.0 52.0 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 10:13:19 2024

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