Zinc in PDB 1s3g: Crystal Structure of Adenylate Kinase From Bacillus Globisporus

All present enzymatic activity of Crystal Structure of Adenylate Kinase From Bacillus Globisporus:
2.7.4.3;

The structure of Crystal Structure of Adenylate Kinase From Bacillus Globisporus, PDB code: 1s3g 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)	27.49 / 2.25
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.288, 65.288, 94.378, 90.00, 90.00, 120.00
R / Rfree (%)	22.3 / 28.8

The binding sites of Zinc atom in the Crystal Structure of Adenylate Kinase From Bacillus Globisporus (pdb code 1s3g). 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 Crystal Structure of Adenylate Kinase From Bacillus Globisporus, PDB code: 1s3g:

Zinc binding site 1 out of 1 in the Crystal Structure of Adenylate Kinase From Bacillus Globisporus


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Adenylate Kinase From Bacillus Globisporus within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn219 b:33.4 occ:1.00 SG A:CYS130 2.2 33.6 1.0 OD2 A:ASP153 2.2 35.6 1.0 SG A:CYS133 2.3 37.5 1.0 SG A:CYS150 2.4 32.8 1.0 OD1 A:ASP153 2.8 34.5 1.0 CG A:ASP153 2.8 38.1 1.0 CB A:CYS130 3.1 27.1 1.0 CB A:CYS133 3.1 35.4 1.0 CB A:CYS150 3.2 24.7 1.0 N A:CYS133 3.5 38.3 1.0 CA A:CYS133 3.9 35.6 1.0 O A:HOH314 4.1 64.0 1.0 CB A:ASP153 4.3 39.6 1.0 CB A:VAL132 4.4 40.4 1.0 C A:VAL132 4.5 38.8 1.0 N A:ASP153 4.5 39.3 1.0 CA A:CYS130 4.5 33.7 1.0 CB A:LYS152 4.6 44.0 1.0 C A:CYS133 4.6 35.2 1.0 CA A:CYS150 4.7 33.7 1.0 CA A:VAL132 4.8 38.8 1.0 N A:VAL132 4.9 40.7 1.0 N A:GLY134 4.9 36.2 1.0 CB A:THR135 4.9 36.2 1.0 CG1 A:VAL132 4.9 33.0 1.0 CA A:ASP153 5.0 38.9 1.0 C A:CYS130 5.0 35.9 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