Magnesium in PDB 9erv: Structure of Salmonella Caprel Bound to BAS11 GP54

The structure of Structure of Salmonella Caprel Bound to BAS11 GP54, PDB code: 9erv was solved by A.Garcia-Pino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.13 / 2.25
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	49.695, 103.264, 209.235, 90, 90, 90
R / Rfree (%)	19.9 / 24.4

The structure of Structure of Salmonella Caprel Bound to BAS11 GP54 also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Magnesium atom in the Structure of Salmonella Caprel Bound to BAS11 GP54 (pdb code 9erv). 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 Structure of Salmonella Caprel Bound to BAS11 GP54, PDB code: 9erv:

Magnesium binding site 1 out of 1 in the Structure of Salmonella Caprel Bound to BAS11 GP54


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Salmonella Caprel Bound to BAS11 GP54 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:28.7 occ:1.00 OD2 A:ASP111 2.2 30.2 1.0 O1B A:ATP402 2.5 33.4 1.0 O1G A:ATP402 2.6 37.9 1.0 O3B A:ATP402 3.2 35.8 1.0 CG A:ASP111 3.3 27.8 1.0 PB A:ATP402 3.4 33.6 1.0 O A:HOH765 3.4 66.5 1.0 PG A:ATP402 3.4 37.7 1.0 CB A:ASP111 4.0 21.2 1.0 NZ A:LYS81 4.0 24.7 1.0 O2B A:ATP402 4.0 33.8 1.0 OD1 A:ASP111 4.2 29.4 1.0 NH2 A:ARG79 4.4 18.0 1.0 OE1 A:GLU180 4.5 31.2 1.0 O2G A:ATP402 4.5 38.3 1.0 N7 A:ATP402 4.5 20.2 1.0 O3G A:ATP402 4.5 37.5 1.0 O A:HOH714 4.6 60.0 1.0 OE2 A:GLU180 4.6 32.5 1.0 O3A A:ATP402 4.7 31.7 1.0 C8 A:ATP402 4.8 20.9 1.0 O A:HOH630 4.9 41.6 1.0 NE2 A:GLN182 4.9 7.5 1.0 CD A:GLU180 4.9 29.5 1.0

T.Zhang, A.Cepauskas, A.Nadieina, A.Thureau, K.Coppieters 't Wallant, C.Martens, D.C.Lim, A.Garcia-Pino, M.T.Laub. A Bacterial Immunity Protein Directly Senses Two Disparate Phage Proteins. Nature 2024.
ISSN: ESSN 1476-4687
PubMed: 39415022
DOI: 10.1038/S41586-024-08039-Y