Magnesium in PDB 9khq: Crystal Structure of N-Acyl Homoserine Lactonase Ahlx

All present enzymatic activity of Crystal Structure of N-Acyl Homoserine Lactonase Ahlx:
3.1.1.81;

The structure of Crystal Structure of N-Acyl Homoserine Lactonase Ahlx, PDB code: 9khq was solved by Y.Chen, X.H.Chu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.20
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	143.141, 143.141, 85.053, 90, 90, 90
R / Rfree (%)	16.4 / 21

The structure of Crystal Structure of N-Acyl Homoserine Lactonase Ahlx also contains other interesting chemical elements:

Nickel

(Ni)

6 atoms

The binding sites of Magnesium atom in the Crystal Structure of N-Acyl Homoserine Lactonase Ahlx (pdb code 9khq). 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 N-Acyl Homoserine Lactonase Ahlx, PDB code: 9khq:

Magnesium binding site 1 out of 1 in the Crystal Structure of N-Acyl Homoserine Lactonase Ahlx


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 N-Acyl Homoserine Lactonase Ahlx within 5.0Å range: probe atom residue distance (Å) B Occ C:Mg303 b:30.0 occ:1.00 CD2 C:HIS158 2.6 55.9 1.0 CD2 A:HIS158 3.1 54.8 1.0 CD2 B:HIS158 3.3 36.5 1.0 CG C:HIS158 3.3 54.1 1.0 CB C:HIS158 3.5 41.0 1.0 CG A:HIS158 3.7 51.5 1.0 NE2 C:HIS158 3.8 55.7 1.0 CB A:HIS158 3.9 37.0 1.0 CA A:HIS158 3.9 33.8 1.0 CA C:HIS158 3.9 32.5 1.0 NE2 A:HIS158 4.1 52.8 1.0 NE2 B:HIS158 4.1 37.6 1.0 O C:HIS158 4.1 32.2 1.0 CG B:HIS158 4.2 43.2 1.0 O A:HIS158 4.3 28.5 1.0 C C:HIS158 4.5 30.9 1.0 C A:HIS158 4.5 30.5 1.0 CA B:HIS158 4.5 32.5 1.0 ND1 C:HIS158 4.6 57.7 1.0 CB B:HIS158 4.6 34.7 1.0 O A:HOH471 4.6 34.3 1.0 ND1 A:HIS158 4.7 49.5 1.0 CE1 C:HIS158 4.8 54.0 1.0 O B:HIS158 4.9 31.1 1.0 CE1 A:HIS158 4.9 44.1 1.0

Y.Chen, X.Xie, J.Zhou, L.Dai, X.Chu, P.Liu. An Ahl-Lactonase Mutant Featuring A Unique "Tri-His" Motif Exhibits Enhanced Activity, Stability and Effectively Controls Plant Soft Rot. Int.J.Biol.Macromol. V. 308 42543 2025.
ISSN: ISSN 0141-8130
PubMed: 40157672
DOI: 10.1016/J.IJBIOMAC.2025.142543