Zinc in PDB 7nu1: Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant

All present enzymatic activity of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant:
6.1.1.4;

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant, PDB code: 7nu1 was solved by L.Pang, S.V.Strelkov, S.D.Weeks, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.94 / 2.51
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.049, 81.876, 226.159, 90, 90, 90
R / Rfree (%)	20.4 / 26.2

The structure of Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant (pdb code 7nu1). 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 Neisseria Gonorrhoeae Leurs E169G Mutant, PDB code: 7nu1:

Zinc binding site 1 out of 1 in the Crystal Structure of Neisseria Gonorrhoeae Leurs E169G Mutant


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 Neisseria Gonorrhoeae Leurs E169G Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn901 b:56.9 occ:1.00 SG A:CYS493 2.4 49.8 1.0 SG A:CYS452 2.4 47.5 1.0 SG A:CYS490 2.4 48.2 1.0 SG A:CYS449 2.4 48.7 1.0 CB A:CYS490 3.1 52.2 1.0 CB A:CYS493 3.2 38.7 1.0 CB A:CYS452 3.3 41.2 1.0 CB A:CYS449 3.4 43.5 1.0 N A:CYS493 3.7 45.6 1.0 N A:CYS452 4.0 44.5 1.0 CA A:CYS493 4.0 38.4 1.0 CA A:CYS452 4.3 38.4 1.0 CB A:CYS492 4.5 46.5 1.0 CA A:CYS490 4.5 40.6 1.0 C A:CYS492 4.6 48.4 1.0 CB A:LYS451 4.7 46.6 1.0 C A:CYS493 4.8 44.9 1.0 C A:LYS451 4.8 57.5 1.0 N A:GLY494 4.8 40.8 1.0 CA A:CYS449 4.8 42.9 1.0 CA A:CYS492 4.9 45.1 1.0 N A:CYS492 4.9 46.8 1.0

L.Pang, V.Zanki, S.V.Strelkov, A.Van Aerschot, I.Gruic-Sovulj, S.D.Weeks. Partitioning of the Initial Catalytic Steps of Leucyl-Trna Synthetase Is Driven By An Active Site Peptide-Plane Flip. Commun Biol V. 5 883 2022.
ISSN: ESSN 2399-3642
PubMed: 36038645
DOI: 10.1038/S42003-022-03825-8