Magnesium in PDB 8yd0: Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib

All present enzymatic activity of Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib:
3.4.21.92;

The binding sites of Magnesium atom in the Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib (pdb code 8yd0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib, PDB code: 8yd0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:30.0 occ:1.00 OG1 A:THR128 1.9 85.7 1.0 O2B A:ATP502 1.9 96.8 1.0 O3G A:ATP502 2.4 96.8 1.0 CB A:THR128 3.0 85.7 1.0 PB A:ATP502 3.1 96.8 1.0 O3B A:ATP502 3.3 96.8 1.0 PG A:ATP502 3.5 96.8 1.0 NH2 B:ARG307 3.6 87.4 1.0 OD1 A:ASP186 3.6 92.3 1.0 N A:THR128 3.9 85.7 1.0 O3A A:ATP502 3.9 96.8 1.0 O2A A:ATP502 3.9 96.8 1.0 CG2 A:THR128 3.9 85.7 1.0 CA A:THR128 4.0 85.7 1.0 OD2 A:ASP186 4.0 92.3 1.0 OE1 A:GLN187 4.1 95.5 1.0 OE1 B:GLU218 4.1 85.5 1.0 NZ A:LYS127 4.2 89.8 1.0 CG A:ASP186 4.2 92.3 1.0 O1B A:ATP502 4.4 96.8 1.0 PA A:ATP502 4.4 96.8 1.0 O2G A:ATP502 4.4 96.8 1.0 OE2 B:GLU218 4.5 85.5 1.0 NH2 A:ARG370 4.5 91.4 1.0 O1G A:ATP502 4.5 96.8 1.0 O1A A:ATP502 4.7 96.8 1.0 CD B:GLU218 4.8 85.5 1.0 CZ B:ARG307 4.9 87.4 1.0 OH A:TYR184 4.9 87.5 1.0 CB A:LYS127 5.0 89.8 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of M. Tuberculosis CLPXP1P2 Complex Bound to Bortezomib within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg502 b:30.0 occ:1.00 O3B E:ADP501 1.3 20.0 1.0 NZ E:LYS127 1.5 85.5 1.0 PB E:ADP501 2.3 20.0 1.0 CE E:LYS127 2.6 85.5 1.0 O2B E:ADP501 2.6 20.0 1.0 OE2 F:GLU303 2.7 109.8 1.0 O1B E:ADP501 3.3 20.0 1.0 O3A E:ADP501 3.5 20.0 1.0 CD E:LYS127 3.7 85.5 1.0 CD F:GLU303 3.8 109.8 1.0 N E:GLY124 3.9 92.3 1.0 OG1 E:THR123 3.9 94.2 1.0 CA E:THR123 4.0 94.2 1.0 OE1 E:GLN187 4.1 98.1 1.0 CG F:GLU303 4.3 109.8 1.0 CB E:THR123 4.4 94.2 1.0 C E:THR123 4.5 94.2 1.0 CG E:LYS127 4.8 85.5 1.0 OE1 F:GLU303 4.8 109.8 1.0 CG2 E:THR128 4.9 80.4 1.0 O E:PRO122 4.9 94.6 1.0 CA E:GLY124 4.9 92.3 1.0 PA E:ADP501 4.9 20.0 1.0

B.Zhou, H.Zhao, Y.Gao, X.Chen, T.Zhang, J.He, X.Xiong. Activation Mechanism of Caseinolytic Chaperone-Protease System in Mycobacterium Tuberculosis By the Anti-Cancer Drug Bortezomib To Be Published.