Magnesium in PDB 6hyy: Human Phosphoserine Phosphatase with Serine and Phosphate

All present enzymatic activity of Human Phosphoserine Phosphatase with Serine and Phosphate:
3.1.3.3;

The structure of Human Phosphoserine Phosphatase with Serine and Phosphate, PDB code: 6hyy was solved by J.Wouters, M.Haufroid, M.Mirgaux, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.95 / 1.57
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	49.140, 129.140, 155.790, 90.00, 90.00, 90.00
R / Rfree (%)	19.5 / 22.6

The structure of Human Phosphoserine Phosphatase with Serine and Phosphate also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the Human Phosphoserine Phosphatase with Serine and Phosphate (pdb code 6hyy). 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 Human Phosphoserine Phosphatase with Serine and Phosphate, PDB code: 6hyy:

Magnesium binding site 1 out of 1 in the Human Phosphoserine Phosphatase with Serine and Phosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Phosphoserine Phosphatase with Serine and Phosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:17.1 occ:1.00 O A:HOH515 2.0 33.6 1.0 OD2 A:ASP20 2.2 28.5 1.0 O A:HOH453 2.2 24.8 1.0 O A:HOH455 2.2 30.0 1.0 OD1 A:ASP179 2.3 24.9 1.0 O A:ASP22 2.3 21.1 1.0 CG A:ASP20 3.0 22.6 1.0 OD1 A:ASP20 3.1 25.7 1.0 CG A:ASP179 3.3 25.2 1.0 C A:ASP22 3.5 20.9 1.0 OD2 A:ASP179 3.6 26.7 1.0 CB A:SER303 4.0 37.8 1.0 OD2 A:ASP183 4.0 26.7 1.0 OE2 A:GLU29 4.1 38.2 1.0 CB A:ASP22 4.2 24.4 1.0 CA A:ASP22 4.2 21.6 1.0 O1 A:PO4301 4.3 45.0 1.0 N A:ASP22 4.3 21.8 1.0 OG1 A:THR24 4.4 20.7 1.0 O A:SER303 4.4 46.1 1.0 O A:HOH404 4.4 46.8 1.0 CB A:ASP20 4.4 19.9 1.0 CB A:SER23 4.4 23.0 1.0 OG A:SER303 4.5 32.8 1.0 N A:SER23 4.5 19.8 1.0 CB A:ASP179 4.6 20.0 1.0 NZ A:LYS158 4.7 33.3 1.0 N A:ASP179 4.7 20.0 1.0 CA A:SER23 4.8 20.2 1.0 N A:GLY180 4.9 20.9 1.0 N A:THR24 4.9 20.6 1.0 C A:SER23 5.0 18.7 1.0 O A:HOH402 5.0 46.1 1.0 CG A:ASP183 5.0 25.6 1.0 OG A:SER23 5.0 27.5 1.0

M.Haufroid, M.Mirgaux, L.Leherte, J.Wouters. Crystal Structures and Snapshots Along the Reaction Pathway of Human Phosphoserine Phosphatase. Acta Crystallogr D Struct V. 75 592 2019BIOL.
ISSN: ISSN 2059-7983
PubMed: 31205021
DOI: 10.1107/S2059798319006867