Magnesium in PDB 8v2j: Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp

The binding sites of Magnesium atom in the Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp (pdb code 8v2j). 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 ALPHA1B and Betai/Ivb Microtubule Bound to Gdp, PDB code: 8v2j:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:89.6 occ:1.00 O2B A:GTP501 2.0 100.7 1.0 O1G A:GTP501 2.0 101.3 1.0 OE2 A:GLU71 2.4 142.9 1.0 PG A:GTP501 3.1 112.6 1.0 PB A:GTP501 3.1 108.2 1.0 O3G A:GTP501 3.5 115.5 1.0 O3B A:GTP501 3.5 101.1 1.0 NZ B:LYS252 3.6 106.5 1.0 CB A:GLN11 3.6 97.2 1.0 CD A:GLU71 3.6 141.8 1.0 O3A A:GTP501 3.6 106.4 1.0 OD2 A:ASP98 3.8 134.5 1.0 OE1 A:GLN11 3.9 99.3 1.0 N A:GLN11 4.0 96.7 1.0 OD2 A:ASP69 4.2 118.8 1.0 OD1 A:ASP69 4.3 120.5 1.0 OE1 A:GLU71 4.4 138.6 1.0 O2G A:GTP501 4.4 102.5 1.0 CA A:GLN11 4.4 90.3 1.0 O1B A:GTP501 4.4 104.4 1.0 O2A A:GTP501 4.5 109.1 1.0 CG A:GLU71 4.6 139.0 1.0 CG A:ASP69 4.7 119.2 1.0 PA A:GTP501 4.7 120.0 1.0 CG A:ASP98 4.7 134.8 1.0 CD A:GLN11 4.7 97.2 1.0 CG A:GLN11 4.8 95.5 1.0 OD1 A:ASP98 4.8 139.1 1.0 CE B:LYS252 4.9 108.8 1.0 OG1 A:THR145 4.9 125.6 1.0

Magnesium binding site 2 out of 2 in the Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of ALPHA1B and Betai/Ivb Microtubule Bound to Gdp within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg502 b:89.4 occ:1.00 O1G D:GTP501 2.0 118.2 1.0 O2B D:GTP501 2.0 109.7 1.0 OE2 D:GLU71 2.0 142.5 1.0 PG D:GTP501 2.7 122.7 1.0 O3B D:GTP501 3.0 112.5 1.0 PB D:GTP501 3.0 116.5 1.0 O2G D:GTP501 3.0 114.1 1.0 CD D:GLU71 3.2 139.3 1.0 OD2 D:ASP98 3.4 130.7 1.0 OD1 D:ASP69 3.8 116.2 1.0 NZ E:LYS252 3.8 115.2 1.0 O3A D:GTP501 3.9 114.5 1.0 OD2 D:ASP69 3.9 111.4 1.0 OE1 D:GLU71 3.9 137.9 1.0 N D:GLN11 4.0 98.3 1.0 CB D:GLN11 4.1 93.5 1.0 O3G D:GTP501 4.1 114.0 1.0 O1B D:GTP501 4.2 115.4 1.0 CG D:GLU71 4.2 134.7 1.0 OG1 D:THR145 4.2 125.3 1.0 CG D:ASP69 4.3 114.5 1.0 CG D:ASP98 4.3 128.9 1.0 OD1 D:ASP98 4.5 131.6 1.0 CB D:THR145 4.5 115.7 1.0 CA D:GLN11 4.6 94.0 1.0 OE1 D:GLN11 4.7 92.8 1.0 CA D:GLY10 4.8 103.7 1.0 C D:GLY10 4.8 104.3 1.0 CE E:LYS252 4.9 113.2 1.0

E.A.Zehr, A.Roll-Mecak. Cryo-Em Structures of Human A1B/Bi+Bivb and A1A/Biii Microtubules Show Tubulin Tails Link Tubulin Dimers and Shed Light on Isoform Specific Assembly To Be Published.