Magnesium in PDB 3fes: Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile

The structure of Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile, PDB code: 3fes was solved by Y.Kim, C.Tesar, H.Li, G.Cobb, A.Joachimiak, Midwest Center For Structuralgenomics (Mcsg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.55 / 1.82
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	34.690, 68.523, 81.339, 66.91, 86.23, 85.33
R / Rfree (%)	18.7 / 22.2

The binding sites of Magnesium atom in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile (pdb code 3fes). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile, PDB code: 3fes:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile


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 the Atp-Dependent Clp Protease Clpc From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg143 b:32.2 occ:1.00 O A:HOH163 2.9 31.9 1.0 OG1 A:THR6 3.0 21.2 1.0 O A:HOH148 3.1 33.5 1.0 O A:HOH157 3.1 28.5 1.0 N A:THR104 3.4 23.4 1.0 CA A:GLY103 3.5 22.1 1.0 CB A:THR6 3.8 22.8 1.0 CG2 A:THR6 3.8 22.2 1.0 CB A:ARG8 3.8 22.2 1.0 OE2 A:GLU105 4.0 28.3 1.0 C A:GLY103 4.0 22.7 1.0 CG2 A:THR104 4.1 23.8 1.0 OG1 A:THR104 4.2 22.1 1.0 CB A:THR104 4.5 22.8 1.0 CA A:THR104 4.5 23.0 1.0 CD A:ARG8 4.5 28.9 1.0 N A:ALA9 4.5 22.7 1.0 O A:HOH159 4.6 23.3 1.0 CG A:ARG8 4.6 25.0 1.0 CA A:ARG8 4.8 22.5 1.0 N A:GLY103 4.8 22.6 1.0 CD A:GLU105 4.9 30.6 1.0 C A:ARG8 4.9 22.0 1.0 N A:ARG8 5.0 23.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile


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 the Atp-Dependent Clp Protease Clpc From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg144 b:30.1 occ:1.00 O B:HOH175 2.8 28.6 1.0 OG1 B:THR6 3.0 22.5 1.0 O B:HOH169 3.1 27.9 1.0 O B:HOH167 3.2 34.0 1.0 N B:THR104 3.3 22.2 1.0 CA B:GLY103 3.6 21.8 1.0 CB B:ARG8 3.8 22.2 1.0 CB B:THR6 3.8 24.4 1.0 OE1 B:GLU105 3.9 25.7 1.0 CG2 B:THR104 3.9 20.9 1.0 CG2 B:THR6 3.9 21.4 1.0 C B:GLY103 4.0 21.7 1.0 OG1 B:THR104 4.2 22.8 1.0 N B:ALA9 4.4 19.7 1.0 CB B:THR104 4.4 21.7 1.0 CA B:THR104 4.4 22.3 1.0 CD B:ARG8 4.5 31.1 1.0 O B:HOH152 4.6 23.7 1.0 CG B:ARG8 4.7 23.6 1.0 CA B:ARG8 4.7 21.1 1.0 C B:ARG8 4.8 20.7 1.0 CD B:GLU105 4.8 31.5 1.0 N B:GLY103 4.9 22.4 1.0 N B:ARG8 4.9 22.3 1.0 O B:HOH183 4.9 45.5 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg146 b:29.2 occ:1.00 O C:HOH164 2.9 39.8 1.0 O C:HOH147 2.9 26.1 1.0 OG1 C:THR6 3.0 22.6 1.0 O C:HOH151 3.2 24.1 1.0 N C:THR104 3.4 21.3 1.0 CA C:GLY103 3.5 20.3 1.0 CB C:ARG8 3.6 23.3 1.0 CB C:THR6 3.8 23.6 1.0 CG2 C:THR6 3.9 21.4 1.0 C C:GLY103 4.0 22.0 1.0 OE1 C:GLU105 4.0 25.3 1.0 CG2 C:THR104 4.1 21.7 1.0 N C:ALA9 4.2 21.9 1.0 OG1 C:THR104 4.3 21.6 1.0 CD C:ARG8 4.5 32.8 1.0 CG C:ARG8 4.5 27.1 1.0 CA C:THR104 4.5 21.9 1.0 CB C:THR104 4.5 20.9 1.0 O C:HOH161 4.6 28.3 1.0 CA C:ARG8 4.7 23.6 1.0 C C:ARG8 4.7 22.6 1.0 N C:GLY103 4.9 21.2 1.0 CD C:GLU105 4.9 27.0 1.0 CB C:ALA9 5.0 21.2 1.0 N C:ARG8 5.0 22.9 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg144 b:33.1 occ:1.00 OG1 D:THR6 2.9 25.6 1.0 O D:HOH153 3.1 30.3 1.0 O D:HOH147 3.3 29.6 1.0 N D:THR104 3.4 24.1 1.0 CA D:GLY103 3.5 23.8 1.0 CB D:ARG8 3.7 29.6 1.0 CB D:THR6 3.8 26.7 1.0 CG2 D:THR6 3.9 26.8 1.0 C D:GLY103 4.0 25.1 1.0 OE1 D:GLU105 4.0 29.0 1.0 CG2 D:THR104 4.1 26.1 1.0 N D:ALA9 4.3 29.2 1.0 OG1 D:THR104 4.4 27.7 1.0 O D:HOH162 4.5 31.5 1.0 CD D:ARG8 4.5 35.1 1.0 CG D:ARG8 4.6 32.6 1.0 CA D:THR104 4.6 25.0 1.0 CB D:THR104 4.6 24.6 1.0 CA D:ARG8 4.7 29.3 1.0 C D:ARG8 4.8 29.6 1.0 N D:GLY103 4.9 24.6 1.0 CB D:ALA9 4.9 29.3 1.0 CD D:GLU105 4.9 27.6 1.0 N D:ARG8 5.0 28.4 1.0

Y.Kim, C.Tesar, H.Li, G.Cobb, A.Joachimiak. Crystal Structure of the Atp-Dependent Clp Protease Clpc From Clostridium Difficile To Be Published.