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Chlorine in PDB 7aur: Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp

Enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp

All present enzymatic activity of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp:
3.6.1.52; 3.6.1.60;

Protein crystallography data

The structure of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp, PDB code: 7aur 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) 46.87 / 1.65
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 61.958, 61.958, 95.924, 90, 90, 120
R / Rfree (%) 20.9 / 24.2

Other elements in 7aur:

The structure of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp also contains other interesting chemical elements:

Magnesium (Mg) 2 atoms

Chlorine Binding Sites:

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

Chlorine binding site 1 out of 1 in 7aur

Go back to Chlorine Binding Sites List in 7aur
Chlorine binding site 1 out of 1 in the Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Yeast Diphosphoinositol Polyphosphate Phosphohydrolase DDP1 in Complex with Amp-Pnp within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl206

b:41.2
occ:1.00
 NH1 A:ARG32 3.1 44.0 1.0
NZ A:LYS63 3.2 33.9 1.0
O A:HOH360 3.2 35.0 1.0
MG A:MG204 3.2 71.7 1.0
O A:HOH348 3.5 46.3 1.0
CG A:LYS63 3.8 28.8 1.0
NH2 A:ARG32 3.9 48.1 1.0
CG1 A:VAL34 3.9 26.9 1.0
CZ A:ARG32 3.9 43.8 1.0
CG2 A:VAL34 3.9 28.2 1.0
CA A:GLY64 4.0 27.1 1.0
CE A:LYS63 4.0 30.2 1.0
C5' A:ANP201 4.1 51.7 1.0
O A:LYS63 4.2 32.0 1.0
N A:GLY64 4.4 26.2 1.0
O4' A:ANP201 4.4 60.3 1.0
C4' A:ANP201 4.4 57.6 1.0
C A:LYS63 4.4 27.9 1.0
CD A:LYS63 4.5 29.8 1.0
O1A A:ANP201 4.5 41.4 1.0
CE1 A:PHE132 4.5 30.3 1.0
CB A:VAL34 4.5 27.1 1.0
C A:GLY64 4.6 26.4 1.0
O A:HOH352 4.8 48.4 1.0
N A:GLY65 4.8 29.0 1.0
CB A:LYS63 4.9 25.9 1.0
O A:HOH349 5.0 43.2 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: Mon Jul 29 18:42:52 2024

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