Zinc in PDB 5x6j: Crystal Structure of B. Globisporus Adenylate Kinase Variant

All present enzymatic activity of Crystal Structure of B. Globisporus Adenylate Kinase Variant:
2.7.4.3;

The structure of Crystal Structure of B. Globisporus Adenylate Kinase Variant, PDB code: 5x6j was solved by S.Moon, E.Bae, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.10
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	65.106, 65.106, 94.565, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 27.6

The binding sites of Zinc atom in the Crystal Structure of B. Globisporus Adenylate Kinase Variant (pdb code 5x6j). 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 B. Globisporus Adenylate Kinase Variant, PDB code: 5x6j:

Zinc binding site 1 out of 1 in the Crystal Structure of B. Globisporus Adenylate Kinase Variant


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 B. Globisporus Adenylate Kinase Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:33.6 occ:1.00 SG A:CYS130 2.2 30.1 1.0 SG A:CYS133 2.3 33.3 1.0 OD2 A:ASP153 2.3 35.2 1.0 SG A:CYS150 2.4 34.3 1.0 OD1 A:ASP153 2.7 33.1 1.0 CG A:ASP153 2.8 34.6 1.0 CB A:CYS150 3.1 34.9 1.0 CB A:CYS130 3.2 32.9 1.0 CB A:CYS133 3.2 30.8 1.0 N A:CYS133 3.5 33.2 1.0 CA A:CYS133 3.9 32.7 1.0 O A:HOH401 4.1 34.3 1.0 CB A:ASP153 4.3 35.8 1.0 CB A:VAL132 4.3 36.9 1.0 CB A:LYS152 4.4 38.8 1.0 N A:ASP153 4.4 31.9 1.0 C A:VAL132 4.5 37.3 1.0 CA A:CYS150 4.6 33.7 1.0 CA A:CYS130 4.6 33.5 1.0 C A:CYS133 4.7 33.9 1.0 CD A:LYS152 4.8 46.2 1.0 CA A:VAL132 4.8 41.0 1.0 N A:GLY134 4.8 34.3 1.0 CG1 A:VAL132 4.8 39.2 1.0 N A:VAL132 4.9 38.4 1.0 CB A:THR135 4.9 40.0 1.0 OG1 A:THR135 4.9 50.6 1.0 N A:GLY155 4.9 39.0 1.0 CA A:ASP153 4.9 34.0 1.0

S.Moon, J.Kim, J.Koo, E.Bae. Structural and Mutational Analyses of Psychrophilic and Mesophilic Adenylate Kinases Highlight the Role of Hydrophobic Interactions in Protein Thermal Stability. Struct Dyn. V. 6 24702 2019.
ISSN: ESSN 2329-7778
PubMed: 31111079
DOI: 10.1063/1.5089707