Magnesium in PDB 1f2u: Crystal Structure of RAD50 Abc-Atpase

The structure of Crystal Structure of RAD50 Abc-Atpase, PDB code: 1f2u was solved by K.P.Hopfner, A.Karcher, D.S.Shin, L.Craig, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	79.900, 82.600, 106.000, 90.00, 90.00, 90.00
R / Rfree (%)	23.8 / 28.2

The binding sites of Magnesium atom in the Crystal Structure of RAD50 Abc-Atpase (pdb code 1f2u). 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 RAD50 Abc-Atpase, PDB code: 1f2u:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of RAD50 Abc-Atpase


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 RAD50 Abc-Atpase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:52.9 occ:1.00 O1B A:ATP901 2.0 49.4 1.0 OG A:SER37 2.0 50.4 1.0 O A:HOH914 2.0 43.3 1.0 O1G A:ATP901 2.1 44.3 1.0 O B:HOH48 2.1 43.9 1.0 OE1 A:GLN140 2.1 47.1 1.0 CD A:GLN140 3.0 45.1 1.0 CB A:SER37 3.2 52.3 1.0 NE2 A:GLN140 3.3 45.3 1.0 PB A:ATP901 3.3 49.6 1.0 PG A:ATP901 3.3 46.1 1.0 O3B A:ATP901 3.6 46.6 1.0 N A:SER37 3.9 53.3 1.0 OD1 B:ASP822 3.9 49.1 1.0 CA A:SER37 4.1 52.9 1.0 OE2 B:GLU823 4.1 46.4 1.0 OD2 B:ASP822 4.1 47.9 1.0 O2A A:ATP901 4.1 52.7 1.0 O3G A:ATP901 4.2 44.7 1.0 O3A A:ATP901 4.2 49.6 1.0 O2B A:ATP901 4.3 50.6 1.0 CG A:GLN140 4.4 45.5 1.0 O A:HOH904 4.4 51.1 1.0 O2G A:ATP901 4.4 42.7 1.0 CG B:ASP822 4.4 49.9 1.0 N D:GLY794 4.4 43.7 1.0 CB A:LYS36 4.6 54.1 1.0 CG B:GLU823 4.6 48.9 1.0 PA A:ATP901 4.7 52.4 1.0 CB A:GLN140 4.7 44.1 1.0 CE A:LYS36 4.7 56.9 1.0 CD B:GLU823 4.9 46.7 1.0 C A:LYS36 5.0 53.1 1.0 CA D:GLY794 5.0 43.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of RAD50 Abc-Atpase


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 RAD50 Abc-Atpase within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg902 b:43.9 occ:1.00 OG C:SER37 2.0 36.7 1.0 O1B C:ATP901 2.0 42.5 1.0 O D:HOH50 2.0 40.6 1.0 OE1 C:GLN140 2.1 41.8 1.0 O C:HOH919 2.1 40.1 1.0 O1G C:ATP901 2.1 37.6 1.0 CD C:GLN140 3.0 38.9 1.0 CB C:SER37 3.1 40.5 1.0 PB C:ATP901 3.4 41.4 1.0 NE2 C:GLN140 3.4 38.3 1.0 PG C:ATP901 3.4 39.9 1.0 O3B C:ATP901 3.7 37.4 1.0 N C:SER37 3.9 40.0 1.0 OD1 D:ASP822 4.0 39.9 1.0 O C:HOH904 4.0 40.4 1.0 CA C:SER37 4.1 39.6 1.0 O2A C:ATP901 4.1 38.2 1.0 OD2 D:ASP822 4.1 41.1 1.0 O3A C:ATP901 4.2 40.6 1.0 O3G C:ATP901 4.2 39.1 1.0 N B:GLY794 4.3 39.9 1.0 CG C:GLN140 4.4 37.8 1.0 CG D:ASP822 4.5 39.3 1.0 O2B C:ATP901 4.5 41.8 1.0 O2G C:ATP901 4.5 37.1 1.0 OE2 D:GLU823 4.6 42.9 1.0 PA C:ATP901 4.6 42.5 1.0 CB C:GLN140 4.7 38.8 1.0 CG D:GLU823 4.8 41.0 1.0 CA B:GLY794 4.8 39.2 1.0 CB C:LYS36 4.9 40.5 1.0 NZ C:LYS36 4.9 41.5 1.0

K.P.Hopfner, A.Karcher, D.S.Shin, L.Craig, L.M.Arthur, J.P.Carney, J.A.Tainer. Structural Biology of RAD50 Atpase: Atp-Driven Conformational Control in Dna Double-Strand Break Repair and the Abc-Atpase Superfamily. Cell(Cambridge,Mass.) V. 101 789 2000.
ISSN: ISSN 0092-8674
PubMed: 10892749
DOI: 10.1016/S0092-8674(00)80890-9