Magnesium in PDB 7b1k: Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate.

All present enzymatic activity of Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate.:
2.7.8.8;

The structure of Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate., PDB code: 7b1k was solved by O.Yildiz, M.Centola, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	57.00 / 2.20
Space group	P 2 21 21
Cell size a, b, c (Å), α, β, γ (°)	62.314, 70.758, 95.545, 90, 90, 90
R / Rfree (%)	25.4 / 30.7

The structure of Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate. also contains other interesting chemical elements:

Calcium	(Ca)	2 atoms
Sodium	(Na)	2 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Magnesium atom in the Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate. (pdb code 7b1k). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate., PDB code: 7b1k:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg303 b:49.5 occ:1.00 OD1 A:ASP41 2.1 65.2 1.0 O A:ASP62 2.2 45.5 1.0 OD1 A:ASP66 2.3 52.3 1.0 O A:HOH401 2.3 58.2 1.0 OG A:SER65 2.5 54.3 1.0 C A:ASP62 3.2 37.7 1.0 CG A:ASP41 3.2 62.7 1.0 CB A:SER65 3.3 34.2 1.0 OD1 A:ASN18 3.3 51.6 1.0 OD1 A:ASP62 3.4 57.0 1.0 CG A:ASP66 3.5 62.3 1.0 N A:ASP66 3.6 50.2 1.0 CG A:ASP62 3.6 64.3 1.0 CA A:ASP62 3.7 30.2 1.0 O A:HOH403 3.7 52.2 1.0 OD2 A:ASP62 3.9 54.2 1.0 CA A:CA302 3.9 47.3 1.0 OD2 A:ASP41 3.9 59.7 1.0 C A:SER65 4.0 39.7 1.0 CA A:SER65 4.1 28.6 1.0 CB A:ASP41 4.1 39.8 1.0 CB A:ASP62 4.2 43.0 1.0 CA A:ASP66 4.3 25.5 1.0 CB A:ASP66 4.3 31.1 1.0 OD2 A:ASP66 4.3 63.9 1.0 N A:SER63 4.4 45.6 1.0 OD2 A:ASP44 4.4 33.7 1.0 N A:SER65 4.5 45.0 1.0 CG A:ASN18 4.5 47.8 1.0 CA A:ASP41 4.7 41.6 1.0 O A:LEU61 4.8 39.6 1.0 CA A:SER63 4.8 42.0 1.0 O A:SER65 4.8 47.4 1.0 CG2 A:THR15 5.0 28.0 1.0 N A:ASP62 5.0 37.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Phosphatidyl Serine Synthase (Pss) in the Closed Conformation with Bound Citrate. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg303 b:50.9 occ:1.00 OD1 B:ASP66 2.0 53.2 1.0 O B:HOH407 2.1 48.5 1.0 O B:ASP62 2.3 35.2 1.0 OD1 B:ASP62 2.7 50.0 1.0 CG B:ASP66 3.1 50.0 1.0 CB B:SER65 3.2 41.9 1.0 OD2 B:ASP41 3.3 63.9 1.0 N B:ASP66 3.3 43.1 1.0 C B:ASP62 3.3 42.5 1.0 OD1 B:ASN18 3.5 45.9 1.0 OG B:SER65 3.7 57.7 1.0 C B:SER65 3.7 39.4 1.0 O B:HOH402 3.7 54.3 1.0 CA B:ASP62 3.7 32.8 1.0 CG B:ASP62 3.7 41.4 1.0 CG B:ASP41 3.8 61.9 1.0 OD2 B:ASP66 3.8 56.9 1.0 CA B:SER65 3.9 26.3 1.0 CA B:ASP66 3.9 26.4 1.0 CB B:ASP66 4.0 35.8 1.0 OD1 B:ASP41 4.1 70.8 1.0 N B:SER65 4.3 39.2 1.0 CB B:ASP62 4.3 36.9 1.0 OD2 B:ASP44 4.4 53.5 1.0 O B:SER65 4.5 48.8 1.0 CA B:CA302 4.5 55.5 1.0 N B:SER63 4.5 46.1 1.0 CB B:ASP41 4.6 36.0 1.0 O B:LEU61 4.7 33.3 1.0 OD2 B:ASP62 4.7 46.7 1.0 CG B:ASN18 4.7 42.7 1.0 CE2 B:PHE70 4.9 24.7 1.0 CA B:SER63 4.9 32.9 1.0 N B:ASP62 5.0 41.2 1.0

M.Centola, H.Betz, O.Yildiz. Crystal Structures of Phosphatidyl Serine Synthase Pss Reveal the Catalytic Mechanism of Cdp-Dag Alcohol O-Phosphatidyl Transferases Nat Commun V. 12 6982 2021.
ISSN: ESSN 2041-1723
DOI: 10.1038/S41467-021-27281-W