Magnesium in PDB 1jbk: Crystal Structure of the First Nucelotide Binding Domain of Clpb

The structure of Crystal Structure of the First Nucelotide Binding Domain of Clpb, PDB code: 1jbk was solved by L.Jingzhi, S.Bingdong, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	38.488, 65.686, 79.087, 90.00, 90.00, 90.00
R / Rfree (%)	22.2 / 24.7

The binding sites of Magnesium atom in the Crystal Structure of the First Nucelotide Binding Domain of Clpb (pdb code 1jbk). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the First Nucelotide Binding Domain of Clpb, PDB code: 1jbk:

Magnesium binding site 1 out of 1 in the Crystal Structure of the First Nucelotide Binding Domain of Clpb


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 First Nucelotide Binding Domain of Clpb within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1 b:19.8 occ:1.00 N A:LYS212 3.5 11.1 1.0 N A:GLY209 3.6 18.6 1.0 N A:GLY211 3.6 15.7 1.0 NZ A:LYS212 3.7 14.9 1.0 O A:HOH516 3.9 32.6 1.0 N A:VAL210 4.0 14.7 1.0 CA A:GLY209 4.1 18.0 1.0 CA A:GLY211 4.1 14.2 1.0 CB A:LYS212 4.3 11.9 1.0 C A:GLY211 4.3 14.3 1.0 C A:GLY209 4.3 18.1 1.0 CG A:LYS212 4.3 13.4 1.0 CA A:LYS212 4.4 10.9 1.0 N A:THR213 4.4 12.8 1.0 O A:HOH490 4.5 34.8 1.0 O A:HOH639 4.5 23.2 1.0 C A:PRO208 4.6 17.9 1.0 O A:HOH492 4.6 29.4 1.0 C A:VAL210 4.7 13.9 1.0 CG2 A:VAL210 4.7 18.6 1.0 O A:GLU207 4.7 14.2 1.0 CA A:PRO208 4.8 18.0 1.0 CG2 A:THR213 4.8 16.9 1.0 CA A:VAL210 4.9 14.8 1.0 CE A:LYS212 4.9 20.0 1.0 OG1 A:THR213 5.0 19.0 1.0 CD A:LYS212 5.0 16.4 1.0 C A:LYS212 5.0 10.7 1.0

J.Li, B.Sha. Crystal Structure of E. Coli HSP100 Clpb Nucleotide-Binding Domain 1 (NBD1) and Mechanistic Studies on Clpb Atpase Activity. J.Mol.Biol. V. 318 1127 2002.
ISSN: ISSN 0022-2836
PubMed: 12054807
DOI: 10.1016/S0022-2836(02)00188-2