Magnesium in PDB 1ksf: Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains

The structure of Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains, PDB code: 1ksf was solved by F.Guo, M.R.Maurizi, L.Esser, D.Xia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.60
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	124.107, 124.107, 97.042, 90.00, 90.00, 120.00
R / Rfree (%)	21.6 / 30.4

The binding sites of Magnesium atom in the Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains (pdb code 1ksf). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains, PDB code: 1ksf:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains


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 Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains within 5.0Å range: probe atom residue distance (Å) B Occ X:Mg782 b:91.0 occ:1.00 O1B X:ADP781 3.2 61.9 1.0 O3B X:ADP781 3.3 73.5 1.0 CE X:LYS501 3.6 58.7 1.0 NZ X:LYS501 3.7 71.1 1.0 PB X:ADP781 3.8 71.1 1.0 OG1 X:THR604 4.0 42.1 1.0 O X:HOH1073 4.0 78.0 1.0 CB X:THR604 4.0 39.9 1.0 OG1 X:THR502 4.3 43.9 1.0 O2B X:ADP781 4.4 78.0 1.0 CB X:LYS501 4.6 37.9 1.0 CD X:LYS501 4.6 47.5 1.0 CG2 X:THR604 4.9 34.6 1.0 N X:THR605 5.0 46.5 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains


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 Clpa, An HSP100 Chaperone and Regulator of Clpap Protease: Structural Basis of Differences in Function of the Two Aaa+ Atpase Domains within 5.0Å range: probe atom residue distance (Å) B Occ X:Mg783 b:86.5 occ:1.00 OE1 X:GLU565 2.2 48.4 1.0 OG X:SER522 2.4 38.9 1.0 OD1 X:ASP520 2.5 51.0 1.0 OD2 X:ASP520 2.5 46.7 1.0 CG X:ASP520 2.9 47.6 1.0 CD X:GLU565 3.2 54.8 1.0 CB X:SER522 3.4 40.5 1.0 CG X:GLU565 3.7 38.3 1.0 OE2 X:GLU565 4.2 67.0 1.0 CB X:GLU565 4.4 37.8 1.0 CB X:ASP520 4.4 44.9 1.0 N X:SER522 4.4 39.8 1.0 CA X:SER522 4.5 40.0 1.0

F.Guo, M.R.Maurizi, L.Esser, D.Xia. Crystal Structure of Clpa, An HSP100 Chaperone and Regulator of Clpap Protease J.Biol.Chem. V. 277 46743 2002.
ISSN: ISSN 0021-9258
PubMed: 12205096
DOI: 10.1074/JBC.M207796200