Magnesium in PDB 3n2g: Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex

The structure of Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex, PDB code: 3n2g was solved by P.Barbier, A.Dorleans, F.Devred, L.Sanz, D.Allegro, C.Alfonso, M.Knossow, V.Peyrot, J.M.Andreu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 4.00
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	328.553, 328.553, 54.745, 90.00, 90.00, 120.00
R / Rfree (%)	20.9 / 24.1

The binding sites of Magnesium atom in the Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex (pdb code 3n2g). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex, PDB code: 3n2g:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg601 b:46.6 occ:1.00 O2B A:GTP600 1.6 75.9 1.0 O3G A:GTP600 2.0 71.4 1.0 PB A:GTP600 3.0 77.0 1.0 N A:THR145 3.1 79.4 1.0 CA A:GLY144 3.1 79.7 1.0 CG2 A:THR145 3.3 79.7 1.0 N A:GLY144 3.3 79.8 1.0 PG A:GTP600 3.3 71.9 1.0 CB A:ALA99 3.3 79.4 1.0 OD1 A:ASP98 3.5 80.6 1.0 C A:GLY144 3.6 79.6 1.0 NZ B:LYS254 3.6 79.4 1.0 O3A A:GTP600 3.6 76.5 1.0 N A:ASN101 3.7 79.3 1.0 O3B A:GTP600 3.7 74.8 1.0 N A:ALA100 3.9 79.3 1.0 O2G A:GTP600 4.1 71.4 1.0 C A:ALA99 4.1 79.2 1.0 CA A:ALA99 4.1 79.3 1.0 O1B A:GTP600 4.2 76.0 1.0 N A:ALA99 4.2 79.3 1.0 CA A:THR145 4.3 79.5 1.0 CB A:THR145 4.3 79.6 1.0 CA A:ASN101 4.4 79.3 1.0 O1G A:GTP600 4.5 71.7 1.0 C A:ALA100 4.5 79.2 1.0 C A:GLY143 4.5 79.4 1.0 CA A:ALA100 4.6 79.3 1.0 O A:ALA99 4.7 79.2 1.0 CG A:ASP98 4.7 80.0 1.0 OG1 A:THR145 4.8 80.5 1.0 O A:GLY144 4.8 79.6 1.0

Magnesium binding site 2 out of 3 in the Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:81.8 occ:1.00 OE1 B:GLN11 3.0 79.7 1.0 O2A B:GDP600 3.2 79.8 1.0 OD1 B:ASN101 3.5 80.4 1.0 OE2 C:GLU254 3.9 88.4 1.0 O2B B:GDP600 4.0 80.2 1.0 CD B:GLN11 4.3 79.5 1.0 CG B:ASN101 4.3 79.8 1.0 PA B:GDP600 4.3 81.5 1.0 CD C:GLU254 4.4 87.9 1.0 O3A B:GDP600 4.5 81.3 1.0 OE1 C:GLU254 4.6 88.6 1.0 OD2 B:ASP179 4.6 80.5 1.0 ND2 B:ASN101 4.7 79.7 1.0 PB B:GDP600 4.8 80.6 1.0 O1A B:GDP600 4.8 81.6 1.0 O3B B:GDP600 5.0 79.2 1.0 CB B:GLN11 5.0 80.0 1.0

Magnesium binding site 3 out of 3 in the Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Tubulin-Nsc 613863: RB3 Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg601 b:67.2 occ:1.00 O2B C:GTP600 1.8 75.3 1.0 O3G C:GTP600 2.1 73.4 1.0 OD1 C:ASP98 2.9 80.2 1.0 CB C:ALA99 3.0 79.4 1.0 NZ D:LYS254 3.3 79.5 1.0 PB C:GTP600 3.3 76.0 1.0 PG C:GTP600 3.3 73.1 1.0 N C:ALA100 3.3 79.5 1.0 CG2 C:THR145 3.3 79.8 1.0 N C:ASN101 3.4 79.2 1.0 N C:THR145 3.5 79.6 1.0 CA C:GLY144 3.5 79.9 1.0 C C:ALA99 3.6 79.3 1.0 CA C:ALA99 3.6 79.2 1.0 N C:ALA99 3.6 79.2 1.0 O2G C:GTP600 3.6 73.6 1.0 O3B C:GTP600 3.8 74.7 1.0 N C:GLY144 3.8 79.9 1.0 C C:GLY144 4.0 79.8 1.0 CA C:ALA100 4.1 79.5 1.0 CG C:ASP98 4.1 79.8 1.0 O3A C:GTP600 4.2 77.1 1.0 C C:ALA100 4.2 79.3 1.0 O1B C:GTP600 4.3 75.1 1.0 CA C:ASN101 4.3 79.2 1.0 O C:ALA99 4.3 79.2 1.0 CB C:THR145 4.5 79.7 1.0 O1G C:GTP600 4.6 72.3 1.0 CE D:LYS254 4.6 79.7 1.0 CA C:THR145 4.6 79.5 1.0 OD2 C:ASP98 4.7 79.8 1.0 C C:ASP98 4.8 79.4 1.0 N C:ASN102 5.0 79.3 1.0

P.Barbier, A.Dorleans, F.Devred, L.Sanz, D.Allegro, C.Alfonso, M.Knossow, V.Peyrot, J.M.Andreu. Stathmin and Interfacial Microtubule Inhibitors Recognize A Naturally Curved Conformation of Tubulin Dimers. J.Biol.Chem. V. 285 31672 2010.
ISSN: ISSN 0021-9258
PubMed: 20675373
DOI: 10.1074/JBC.M110.141929