Magnesium in PDB 1sa0: Tubulin-Colchicine: Stathmin-Like Domain Complex

The structure of Tubulin-Colchicine: Stathmin-Like Domain Complex, PDB code: 1sa0 was solved by R.B.Ravelli, B.Gigant, P.A.Curmi, I.Jourdain, S.Lachkar, A.Sobel, M.Knossow, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.58
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	328.690, 328.691, 54.679, 90.00, 90.00, 120.00
R / Rfree (%)	23.2 / 24.9

The binding sites of Magnesium atom in the Tubulin-Colchicine: Stathmin-Like Domain Complex (pdb code 1sa0). 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-Colchicine: Stathmin-Like Domain Complex, PDB code: 1sa0:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Tubulin-Colchicine: 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-Colchicine: Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:80.0 occ:1.00 O2B A:GTP600 1.8 83.1 1.0 O3G A:GTP600 2.0 83.1 1.0 CA A:GLY144 3.0 83.1 1.0 PG A:GTP600 3.0 83.1 1.0 O2G A:GTP600 3.0 83.1 1.0 PB A:GTP600 3.1 83.1 1.0 N A:GLY144 3.1 83.1 1.0 CB A:ALA99 3.3 83.1 1.0 O3B A:GTP600 3.5 83.1 1.0 O3A A:GTP600 3.6 83.1 1.0 OD1 A:ASP98 3.6 83.1 1.0 N A:THR145 3.7 83.1 1.0 C A:GLY144 3.9 83.1 1.0 N A:ASN101 3.9 83.1 1.0 CG2 A:THR145 4.0 83.1 1.0 CA A:ASN101 4.2 83.1 1.0 CA A:ALA99 4.3 83.1 1.0 N A:ALA100 4.3 83.1 1.0 C A:ALA99 4.3 83.1 1.0 C A:GLY143 4.4 83.1 1.0 O1B A:GTP600 4.4 83.1 1.0 O1G A:GTP600 4.4 83.1 1.0 N A:ALA99 4.5 83.1 1.0 CE B:LYS254 4.5 83.1 1.0 CG A:ASP98 4.7 83.1 1.0 C A:ALA100 4.7 83.1 1.0 NZ B:LYS254 4.8 83.1 1.0 CG A:ASN101 4.8 83.1 1.0 O A:ALA99 4.9 83.1 1.0 OD1 A:ASN101 4.9 83.1 1.0 CA A:THR145 4.9 83.1 1.0 OD2 A:ASP98 5.0 83.1 1.0 PA A:GTP600 5.0 83.1 1.0 CB A:ASN101 5.0 83.1 1.0

Magnesium binding site 2 out of 3 in the Tubulin-Colchicine: 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-Colchicine: Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg502 b:83.1 occ:1.00 O2A B:GDP602 2.6 83.1 1.0 ND2 B:ASN101 2.9 83.1 1.0 O3B B:GDP602 3.5 83.1 1.0 PA B:GDP602 3.6 83.1 1.0 O3A B:GDP602 3.6 83.1 1.0 OE1 B:GLN11 3.8 83.1 1.0 CG B:ASN101 3.9 83.1 1.0 OD1 B:ASN101 4.0 83.1 1.0 PB B:GDP602 4.1 83.1 1.0 O1A B:GDP602 4.3 83.1 1.0 O2B B:GDP602 4.7 83.1 1.0 CB B:GLN11 4.7 83.1 1.0 OE2 C:GLU254 4.8 83.1 1.0 OE1 C:GLU254 4.9 83.1 1.0 CD B:GLN11 4.9 83.1 1.0 OD2 B:ASP179 4.9 83.1 1.0 OE2 B:GLU71 4.9 83.1 1.0 O5' B:GDP602 5.0 83.1 1.0

Magnesium binding site 3 out of 3 in the Tubulin-Colchicine: 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-Colchicine: Stathmin-Like Domain Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg503 b:83.1 occ:1.00 O3G C:GTP601 1.8 83.1 1.0 O2B C:GTP601 2.0 83.1 1.0 PG C:GTP601 2.8 83.1 1.0 O2G C:GTP601 2.9 83.1 1.0 CA C:GLY144 2.9 83.1 1.0 N C:GLY144 3.1 83.1 1.0 CB C:ALA99 3.2 83.1 1.0 PB C:GTP601 3.2 83.1 1.0 O3B C:GTP601 3.5 83.1 1.0 N C:THR145 3.5 83.1 1.0 OD1 C:ASP98 3.6 83.1 1.0 O3A C:GTP601 3.7 83.1 1.0 C C:GLY144 3.8 83.1 1.0 CG2 C:THR145 3.8 83.1 1.0 N C:ASN101 3.9 83.1 1.0 O1G C:GTP601 4.2 83.1 1.0 CE D:LYS254 4.2 83.1 1.0 CA C:ALA99 4.2 83.1 1.0 NZ D:LYS254 4.3 83.1 1.0 CA C:ASN101 4.3 83.1 1.0 N C:ALA100 4.3 83.1 1.0 C C:GLY143 4.4 83.1 1.0 C C:ALA99 4.4 83.1 1.0 N C:ALA99 4.5 83.1 1.0 O1B C:GTP601 4.5 83.1 1.0 CG C:ASP98 4.7 83.1 1.0 CA C:THR145 4.8 83.1 1.0 C C:ALA100 4.9 83.1 1.0 CB C:THR145 5.0 83.1 1.0 OD2 C:ASP98 5.0 83.1 1.0 O C:GLY144 5.0 83.1 1.0

R.B.Ravelli, B.Gigant, P.A.Curmi, I.Jourdain, S.Lachkar, A.Sobel, M.Knossow. Insight Into Tubulin Regulation From A Complex with Colchicine and A Stathmin-Like Domain. Nature V. 428 198 2004.
ISSN: ISSN 0028-0836
PubMed: 15014504
DOI: 10.1038/NATURE02393