Zinc in PDB 1p3j: Adenylate Kinase From Bacillus Subtilis

All present enzymatic activity of Adenylate Kinase From Bacillus Subtilis:
2.7.4.3;

The structure of Adenylate Kinase From Bacillus Subtilis, PDB code: 1p3j was solved by E.Bae, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.21 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	32.800, 73.200, 38.100, 90.00, 101.60, 90.00
R / Rfree (%)	19.7 / 24.6

The structure of Adenylate Kinase From Bacillus Subtilis also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Adenylate Kinase From Bacillus Subtilis (pdb code 1p3j). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Adenylate Kinase From Bacillus Subtilis, PDB code: 1p3j:

Zinc binding site 1 out of 1 in the Adenylate Kinase From Bacillus Subtilis


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Adenylate Kinase From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn218 b:36.0 occ:1.00 SG A:CYS130 2.1 29.2 1.0 SG A:CYS150 2.2 31.3 1.0 SG A:CYS133 2.4 36.3 1.0 OD2 A:ASP153 2.4 43.4 1.0 OD1 A:ASP153 2.9 37.5 1.0 CB A:CYS130 2.9 29.6 1.0 CG A:ASP153 2.9 41.3 1.0 CB A:CYS150 3.0 35.1 1.0 CB A:CYS133 3.3 39.9 1.0 N A:CYS133 3.8 42.0 1.0 CG1 A:VAL132 3.8 43.7 1.0 CG2 A:THR135 4.1 37.7 1.0 CA A:CYS133 4.1 40.5 1.0 CB A:ASP153 4.4 44.4 1.0 N A:ASP153 4.4 46.4 1.0 CA A:CYS130 4.4 32.6 1.0 CE A:LYS152 4.4 62.5 1.0 CA A:CYS150 4.5 35.9 1.0 CB A:LYS152 4.6 43.9 1.0 C A:CYS133 4.8 39.1 1.0 C A:VAL132 4.8 43.5 1.0 N A:GLY134 4.9 36.3 1.0 CA A:ASP153 4.9 45.0 1.0 N A:VAL132 4.9 41.8 1.0 C A:CYS130 4.9 36.1 1.0 N A:GLY155 5.0 38.5 1.0 CB A:VAL132 5.0 44.5 1.0

E.Bae, G.N.Phillips Jr.. Structures and Analysis of Highly Homologous Psychrophilic, Mesophilic, and Thermophilic Adenylate Kinases. J.Biol.Chem. V. 279 28202 2004.
ISSN: ISSN 0021-9258
PubMed: 15100224
DOI: 10.1074/JBC.M401865200