Magnesium in PDB 4gni: Structure of the SSZ1 Atpase Bound to Atp and Magnesium

The structure of Structure of the SSZ1 Atpase Bound to Atp and Magnesium, PDB code: 4gni was solved by G.Bange, I.Sinning, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.07 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	80.630, 55.380, 98.790, 90.00, 106.53, 90.00
R / Rfree (%)	20.1 / 24.4

The binding sites of Magnesium atom in the Structure of the SSZ1 Atpase Bound to Atp and Magnesium (pdb code 4gni). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the SSZ1 Atpase Bound to Atp and Magnesium, PDB code: 4gni:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of the SSZ1 Atpase Bound to Atp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the SSZ1 Atpase Bound to Atp and Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:16.6 occ:1.00 O2B A:ATP502 2.1 14.1 1.0 O A:HOH610 2.2 12.2 1.0 O A:HOH603 2.2 13.7 1.0 O A:HOH604 2.3 13.5 1.0 O A:HOH601 2.3 15.1 1.0 O A:HOH612 2.3 17.0 1.0 PB A:ATP502 3.5 14.6 1.0 O1G A:ATP502 3.8 12.8 1.0 O A:HOH605 4.0 16.4 1.0 OD1 A:ASP211 4.0 18.0 1.0 O A:HOH609 4.1 15.0 1.0 OE1 A:GLN390 4.1 15.3 1.0 O2A A:ATP502 4.1 16.8 1.0 O A:HOH621 4.1 20.0 1.0 OD2 A:ASP211 4.2 15.3 1.0 O3B A:ATP502 4.2 15.4 1.0 NE2 A:GLN390 4.2 20.4 1.0 OE2 A:GLU186 4.2 19.0 1.0 O3G A:ATP502 4.2 12.1 1.0 PG A:ATP502 4.3 13.7 1.0 CD A:GLU186 4.4 14.4 1.0 CG A:ASP211 4.5 20.9 1.0 O1B A:ATP502 4.5 16.4 1.0 OE1 A:GLU186 4.5 14.0 1.0 O3A A:ATP502 4.5 19.2 1.0 CD A:GLN390 4.6 19.0 1.0 PA A:ATP502 4.9 16.7 1.0

Magnesium binding site 2 out of 2 in the Structure of the SSZ1 Atpase Bound to Atp and Magnesium


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the SSZ1 Atpase Bound to Atp and Magnesium within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg501 b:11.6 occ:1.00 O2B B:ATP502 2.0 10.2 1.0 O B:HOH603 2.2 9.6 1.0 O B:HOH605 2.2 8.8 1.0 O B:HOH607 2.2 7.2 1.0 O B:HOH628 2.2 10.4 1.0 O B:HOH612 2.3 9.3 1.0 PB B:ATP502 3.4 8.9 1.0 O1G B:ATP502 3.8 7.6 1.0 O B:HOH620 3.9 11.4 1.0 O2A B:ATP502 4.0 10.1 1.0 O B:HOH626 4.0 11.8 1.0 O3B B:ATP502 4.0 8.5 1.0 OD1 B:ASP211 4.1 11.2 1.0 O B:HOH746 4.1 16.3 1.0 O3G B:ATP502 4.1 9.0 1.0 OE1 B:GLN390 4.2 12.1 1.0 OE2 B:GLU186 4.2 13.4 1.0 PG B:ATP502 4.3 7.4 1.0 OD2 B:ASP211 4.3 14.3 1.0 NE2 B:GLN390 4.4 13.5 1.0 O1B B:ATP502 4.4 10.1 1.0 O3A B:ATP502 4.5 12.7 1.0 CD B:GLU186 4.5 12.0 1.0 CG B:ASP211 4.5 13.4 1.0 OE1 B:GLU186 4.6 12.2 1.0 CD B:GLN390 4.7 11.4 1.0 PA B:ATP502 4.8 10.5 1.0 CA B:GLY213 5.0 9.1 1.0

C.Leidig, G.Bange, J.Kopp, S.Amlacher, A.Aravind, S.Wickles, G.Witte, E.Hurt, R.Beckmann, I.Sinning. Structural Characterization of A Eukaryotic Chaperone-the Ribosome-Associated Complex. Nat.Struct.Mol.Biol. V. 20 23 2013.
ISSN: ISSN 1545-9993
PubMed: 23202586
DOI: 10.1038/NSMB.2447