Magnesium in PDB 4c0b: Structure of Wild-Type CLP1P-PCF11P (454-563) Complex

The structure of Structure of Wild-Type CLP1P-PCF11P (454-563) Complex, PDB code: 4c0b was solved by S.Fribourg, A.F.Dupin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.55 / 2.77
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	89.352, 95.410, 182.142, 90.00, 90.00, 90.00
R / Rfree (%)	17.87 / 21.37

The binding sites of Magnesium atom in the Structure of Wild-Type CLP1P-PCF11P (454-563) Complex (pdb code 4c0b). 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 Wild-Type CLP1P-PCF11P (454-563) Complex, PDB code: 4c0b:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Structure of Wild-Type CLP1P-PCF11P (454-563) Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Wild-Type CLP1P-PCF11P (454-563) Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1447 b:67.8 occ:1.00 OG1 A:THR137 2.0 70.8 1.0 O3G A:ATP1446 2.2 0.7 1.0 O1B A:ATP1446 2.4 0.9 1.0 CB A:THR137 3.4 65.5 1.0 PG A:ATP1446 3.5 0.6 1.0 PB A:ATP1446 3.6 1.0 1.0 O3B A:ATP1446 3.7 0.4 1.0 N A:THR137 4.0 62.7 1.0 O2A A:ATP1446 4.2 0.1 1.0 CG2 A:THR137 4.2 61.0 1.0 OD2 A:ASP161 4.2 85.0 1.0 CA A:THR137 4.3 60.0 1.0 O1G A:ATP1446 4.3 0.5 1.0 OE1 A:GLN164 4.4 88.2 1.0 O2G A:ATP1446 4.5 0.7 1.0 CG A:GLN164 4.5 72.6 1.0 O2B A:ATP1446 4.6 0.5 1.0 OD2 A:ASP251 4.6 90.1 1.0 CB A:LYS136 4.6 69.5 1.0 O3A A:ATP1446 4.7 0.2 1.0 NZ A:LYS136 4.7 88.9 1.0 OD1 A:ASP251 4.7 79.8 1.0 CD A:GLN164 4.7 84.7 1.0 CG A:ASP251 4.9 76.1 1.0 CE A:LYS136 4.9 77.5 1.0 C A:LYS136 5.0 67.8 1.0 PA A:ATP1446 5.0 0.9 1.0

Magnesium binding site 2 out of 2 in the Structure of Wild-Type CLP1P-PCF11P (454-563) Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of Wild-Type CLP1P-PCF11P (454-563) Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1448 b:66.8 occ:1.00 O3G B:ATP1447 2.1 0.8 1.0 OG1 B:THR137 2.3 65.8 1.0 O1B B:ATP1447 2.6 0.9 1.0 PG B:ATP1447 3.5 0.9 1.0 CB B:THR137 3.7 58.0 1.0 PB B:ATP1447 3.8 0.3 1.0 O3B B:ATP1447 3.9 0.4 1.0 OD2 B:ASP161 3.9 71.2 1.0 O2G B:ATP1447 4.2 0.6 1.0 N B:THR137 4.3 51.4 1.0 O1G B:ATP1447 4.5 0.4 1.0 CG2 B:THR137 4.5 50.7 1.0 NZ B:LYS136 4.5 97.2 1.0 OE1 B:GLN164 4.5 78.8 1.0 OD2 B:ASP251 4.5 75.0 1.0 CA B:THR137 4.6 50.4 1.0 CG B:GLN164 4.6 60.6 1.0 CB B:LYS136 4.6 59.3 1.0 O2B B:ATP1447 4.6 0.2 1.0 O B:THR252 4.6 50.3 1.0 CE B:LYS136 4.7 79.9 1.0 CG B:ASP161 4.8 63.8 1.0 CD B:GLN164 4.9 81.1 1.0 O2A B:ATP1447 4.9 0.8 1.0 CB B:ASP161 4.9 50.1 1.0 CG B:ASP251 5.0 68.7 1.0

A.F.Dupin, S.Fribourg. Structural Basis For Atp Loss By CLP1P in A G135R Mutant Protein. Biochmie V. 101 203 2014.
ISSN: ISSN 0300-9084
PubMed: 24508575
DOI: 10.1016/J.BIOCHI.2014.01.017